Updated on 2024/10/08

写真a

 
Ara, Katsutoshi
 
Affiliation
Faculty of Science and Engineering, Waseda Research Institute for Science and Engineering
Job title
Senior Researcher(Professor)
Degree
Ph.D. ( 1996.09 Hokkaido University )

Research Experience

  • 2018.10
    -
    Now

    Waseda University

  • 2014.04
    -
    2018.09

    一般財団法人 バイオインダストリー協会（JBA）   先端技術・開発部   部長

  • 1981.04
    -
    2018.09

    花王株式会社（旧 花王石鹸株式会社）   主席研究員

  • 2011.01
    -
    2014.02

    花王（中国）研究開発中心有限公司   基盤研究部   基盤研究部長 （兼）安全性研究室長 （兼）中医学研究室長

Committee Memberships

  • 2020.04
    -
    Now

    新エネルギー・産業技術総合開発機構（NEDO)  技術委員

  • 2020.04
    -
    Now

    バイオインダストリー協会 運営委員会  運営委員

  • 2018.04
    -
    Now

    文部科学省 科学技術・学術政策研究所 科学技術予測センター  専門調査員

  • 2017.06
    -
    Now

    新化学技術推進協会 戦略提言部会  部会委員

  • 2017.04
    -
    Now

    バイオインダストリー協会 発酵と代謝研究会  常任幹事

  • 2017.04
    -
    Now

    バイオインダストリー協会 アルコール・バイオマス研究会  常任幹事

  • 2007.04
    -
    2020

    バイオインダストリー協会 新資源生物変換研究会  幹事

  • 2017
    -
    2018

    NEDO プロジェクト知財委員会  委員

  • 2017
    -
    2018

    日本生物工学会  代議員

  • 2016
    -
    2017

    NEDO スマートセル調査委員会  委員

  • 2012
    -
    2014

    日本農芸化学会  関東支部参与

  • 2011
    -
    2012

    日本農芸化学会  評議員

  • 2010
    -
    2011

    NEDO 多機能集積細胞によるバイオマテリアル生産技術の戦略調査委員会 合成生物工学ワーキンググループ  委員

  • 2010
    -
    2011

    経団連 産業技術委員会 重点化戦略部会  代理委員

  • 2010
    -
    2011

    JBA産業部会  幹事

  • 2010
    -
    2011

    JBA業務委員会委員  委員

  • 2009
    -
    2010

    日本農芸化学会  代議員

  • 2008
    -
    2010

    JBA環境型社会の構築を目指したﾊﾞｲｵﾏｽ産業技術開発調査事業委員会（分科会）  委員

  • 2008
    -
    2010

    JBA網羅的解析技術の適用による微生物利用産業の拡大に向けた課題調査委員会  調査委員

  • 2003
    -
    2009

    日本乳酸菌学会  評議員

  • 2007
    -
    2008

    JBAグリーンバイオ戦略フォーラム バイオマス分科会  幹事

  • 1999
    -
    2006

    石鹸洗剤工業会 除菌試験法策定WG  委員

▼display all

Professional Memberships

  • 　
    -
    Now

    Japan Association for Chemical Innovation

  • 　
    -
    Now

    Japan Bioindustry Association

  • 　
    -
    Now

    Society for Biotechnology, Japan

  • 　
    -
    Now

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

  • 　
    　
    　

    日本乳酸菌学会

  • 　
    　
    　

    Society for Antibacterial and Antifungal Agents, Japan

  • 　
    　
    　

    Japanese Society for Bacteriology

  • 　
    　
    　

    Japanese Society for Medical Mycology

  • 　
    　
    　

    Nihoncha Instructor Association

  • 　
    　
    　

    Institution of Professional Engineers, Japan

▼display all

Research Areas

  • Food sciences / Biofunction and bioprocess engineering / Molecular biology / Applied biochemistry / Applied microbiology

Awards

  • Katsutoshi Ara

    2011   Marquis' Who's Who in Science and Engineerin   11th Edition

  • Katsutoshi Ara

    2009   Marquis’ Who’s Who in America   63rd Edition

  • Katsutoshi Ara

    2008   International Biographical Centre, Cambridge   2000 Outstanding Intellectuals of the 21st Century,

  • Katsutoshi Ara

    2008   Marquis’ Who’s Who in the World   25th Silver Anniversary Edition

  • 荒勝俊

    1985   特許庁   第44回注目発明選定

    Winner： 倉根隆一, 荒勝俊, 中村以正, 鈴木智雄, 福岡誠一

Media Coverage

  • ２年目を迎えた「早稲田地球再生塾」 早稲田理工のSDGｓへの取組み

    Newspaper, magazine

    朝日新聞出版   早稲田理工 by AERA 2020  

    P28-30  

    2020.03

  • 発酵と代謝研究会シンポジウム 「人のインサイ ド空間に迫る～Society5.0+が 実現するヒューマンサスティナブルシステム～」

    Newspaper, magazine

    Author： Myself  

    バイオインダストリー協会   バイオサイエンスとインダストリー  

    JBA news  

    2019.03

  • 異分野の研究者、ビジネスリーダーが集う「早稲田地球再生塾」

    Newspaper, magazine

    朝日新聞出版   早稲田理工 by AERA 2019  

    P32-33  

    2019.03

  • 早稲田地球再生塾第１回勉強会 開催 「住宅・建築物の脱炭素化」に焦点

    Newspaper, magazine

    月刊スマートハウス   Smart House  

    P9  

    2018.09

  • 連載 つなげて広がるリスクコミュニケーション Vol.7 微生物からの恩恵

    Newspaper, magazine

    Author： Myself  

    食品化学新聞社   食品化学新聞  

    2018.06

  • GIF/」ABEX合同シンポジウム 「パイオエコノミーに関する技術開発・屋業 。政策」

    Newspaper, magazine

    Author： Myself  

    バイオインダストリー協会   バイオサイエンスとインダストリー  

    JBA news  

    2018.05

  • 理工系研究組織の新しい姿

    Newspaper, magazine

    朝日新聞出版   早稲田理工 by AERA 2018  

    P30-31  

    2018.03

  • 日本版バイオエコノミーとアカデミアにおけるSDGｓの推進にむけて

    Internet

    Author： Myself  

    日経バイオテク   日経バイオテク  

    バイオエコノミー──日本が選択すべき道──（第6回）  

    2018.01

  • 花王（中国）研究开发中心有限公司与上海交通大学Bio-X研究院成立联合实验室

    Newspaper, magazine

    紫竹国家高新技术产业开发区   紫竹国家高新技术产业开发区新聞  

    http://www.zizhupark.com/news/view/2168  

    2013.04

  • 花王（中国）研究开发中心有限公司与上海交通大学系统生物医学研究院签署合作协议

    Newspaper, magazine

    紫竹国家高新技术产业开发区   紫竹国家高新技术产业开发区  

    http://www.zizhupark.com/news/view/1883  

    2012.01

  • 不要遺伝子除き「細胞工場」改善 花王酵素の生産性２倍に

    日本経済新聞社   日本経済新聞  

    技術ウォッチ  

    2008.09

  • 細菌の浴室の使い方とカビ・酵母の実態と対策

    Promotional material

    花王   KAO-INFORMATION  

    2005.06

  • 最近の浴室の使い方とカビ掃除の実態調査

    Promotional material

    花王株式会社   News Release  

    2005.05

  • カビ②寝室で元気いっぱい

    Newspaper, magazine

    読売新聞社   読売新聞  

    暮らしバイオ研究所  

    2004.04

  • カビ①乾燥した場所も好き

    Newspaper, magazine

    読売新聞社   読売新聞  

    暮らしバイオ研究所  

    2004.04

  • カビ防止には換気と除菌

    Newspaper, magazine

    下野新聞社   下野新聞  

    くらし  

    2003.06

  • 生活者視点にたった家庭の衛生対策

    Promotional material

    花王株式会社   KAO-INFORMATION  

    2003.06

  • カビ対策を調べてみました 掃除と除湿で発生を予防

    朝日新聞社   朝日新聞  

    元気  

    2003.05

  • 水虫菌 体重計にも 共同浴室花王調査

    Newspaper, magazine

    産経新聞社   産経新聞  

    ６面  

    2001.04

  • 水虫感染 体重計にご注意 花王が調査

    Newspaper, magazine

    毎日新聞社   毎日新聞  

    社会面  

    2001.04

  • ツメの垢に秘められた罠を探る

    日本テレビ   発掘！あるある大事典 第145回  

    1998.08

  • アルカリ性でも活性保持 花王、実用化にめど 自動食器洗い機に応用 洗剤用アミラーゼ

    Newspaper, magazine

    化学工業日報  

    1998.04

  • 衣料用漂白剤に酵素を配合、自社生産第３の酵素アミラーゼを実用化《花王》

    Newspaper, magazine

    日経バイオテク社   日経バイオテク  

    1996.07

  • 酵素研究で新展開 アミロプルラナーゼなど新種発見

    日刊工業新聞社   日刊工業新聞  

    わが社のバイオ成果と動向（新春特集）  

    1996.01

  • しつこいデンプン汚れを分解する新酵素を発見

    Newspaper, magazine

    講談社   Quark  

    1995.11

  • バイオ戦略 花王 洗剤用酵素３種の蛋白工学に邁進、来年にも組換え実用化

    Newspaper, magazine

    日経バイオテク   BIO-INTELLIGENCE  

    1995.10

  • 土壌細菌から洗剤用酵素 花王が単離成功 年内にも商品化

    化学工業新聞社   化学工業新聞  

    1995.07

  • でんぷん汚れ効率良く分解 花王が新酵素発見 新洗剤の成分に利用も

    日経産業新聞社   日経産業新聞  

    1995.07

  • 次世代産業基盤技術の研究開発

    Newspaper, magazine

    日刊工業新聞社   TRIGGER トリガー  

    特集  

    1985.08

▼display all

 

Papers

  • Kininogen-Nitric Oxide Signaling at Nearby Nonexcited Acupoints after Long-Term Stimulation.

    Ting Wang, Geng Zhu, Liyue Qin, Qian Wang, Chen She, Dongsheng Xu, Weiwei Hu, Kenghuo Luo, Ying Lei, Yanling Gong, Arijit Ghosh, Dongni Ma, Chun-Lei Ding, Bu-Yi Wang, Yang Guo, Shou-Shan Ma, Michihiro Hattori, Yutaka Takagi, Katsutoshi Ara, Kazuhiko Higuchi, Xingwang Li, Lin He, Wanzhu Bai, Koichi Ishida, Sheng-Tian Li

    JID innovations : skin science from molecules to population health   1 ( 3 ) 100038 - 100038  2021.09  [International journal]

    　View Summary

    Acupuncture treatment is based on acupoint stimulation; however, the biological basis is not understood. We stimulated one acupoint with catgut embedding for 8 weeks and then used isobaric tags for relative and absolute quantitation to screen proteins with altered expression in adjacent acupoints of Sprague Dawley rats. We found that kininogen expression was significantly upregulated in the stimulated and the nonstimulated adjacent acupoints along the same meridian. The enhanced kininogen expression was meridian dependent and was most apparent among small vessels in the subcutaneous layer. Enhanced signals of nitric oxide synthases, cGMP-dependent protein kinase, and myosin light chain were also observed at the nonstimulated adjacent acupoints along the same meridian. These findings uncover biological changes at acupoints and suggest the critical role of the kininogen-nitric oxide signaling pathway in acupoint activation.

    DOI PubMed

    Scopus

  • Improved production of secreted heterologous enzyme in Bacillus subtilis strain MGB874 via modification of glutamate metabolism and growth conditions.

    Kenji Manabe, Yasushi Kageyama, Takuya Morimoto, Eri Shimizu, Hiroki Takahashi, Shigehiko Kanaya, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    Microbial cell factories   12   18 - 18  2013.02  [International journal]

    　View Summary

    BACKGROUND: The Bacillus subtilis genome-reduced strain MGB874 exhibits enhanced production of exogenous extracellular enzymes under batch fermentation conditions. We predicted that deletion of the gene for RocG, a bi-functional protein that acts as a glutamate dehydrogenase and an indirect repressor of glutamate synthesis, would improve glutamate metabolism, leading to further increased enzyme production. However, deletion of rocG dramatically decreased production of the alkaline cellulase Egl-237 in strain MGB874 (strain 874∆rocG). RESULTS: Transcriptome analysis and cultivation profiles suggest that this phenomenon is attributable to impaired secretion of alkaline cellulase Egl-237 and nitrogen starvation, caused by decreased external pH and ammonium depletion, respectively. With NH3-pH auxostat fermentation, production of alkaline cellulase Egl-237 in strain 874∆rocG was increased, exceeding that in the wild-type-background strain 168∆rocG. Notably, in strain 874∆rocG, high enzyme productivity was observed throughout cultivation, possibly due to enhancement of metabolic flux from 2-oxoglutarate to glutamate and generation of metabolic energy through activation of the tricarboxylic acid (TCA) cycle. The level of alkaline cellulase Egl-237 obtained corresponded to about 5.5 g l-1, the highest level reported so far. CONCLUSIONS: We found the highest levels of production of alkaline cellulase Egl-237 with the reduced-genome strain 874∆rocG and using the NH3-pH auxostat. Deletion of the glutamate dehydrogenase gene rocG enhanced enzyme production via a prolonged auxostat fermentation, possibly due to improved glutamate synthesis and enhanced generation of metabolism energy.

    DOI PubMed

    Scopus

    30
    Citation
    (Scopus)

  • Zymography of extracellular protease in Bacillus subtilis.

    T.Kodama, K.Endo, K. Ara, K. Ozaki, J. Sekiguchi

    International Journal of Biosciences and Biotechnology   1 ( 2 ) 60 - 66  2013.01  [Refereed]

  • High external pH enables more efficient secretion of alkaline α-amylase AmyK38 by Bacillus subtilis.

    Kenji Manabe, Yasushi Kageyama, Masatoshi Tohata, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    Microbial cell factories   11   74 - 74  2012.06  [International journal]

    　View Summary

    BACKGROUND: Bacillus subtilis genome-reduced strain MGB874 exhibits enhanced production of exogenous extracellular alkaline cellulase Egl-237 and subtilisin-like alkaline protease M-protease. Here, we investigated the suitability of strain MGB874 for the production of α-amylase, which was anticipated to provoke secretion stress responses involving the CssRS (Control secretion stress Regulator and Sensor) system. RESULTS: Compared to wild-type strain 168, the production of a novel alkaline α-amylase, AmyK38, was severely decreased in strain MGB874 and higher secretion stress responses were also induced. Genetic analyses revealed that these phenomena were attributable to the decreased pH of growth medium as a result of the lowered expression of rocG, encoding glutamate dehydrogenase, whose activity leads to NH3 production. Notably, in both the genome-reduced and wild-type strains, an up-shift of the external pH by the addition of an alkaline solution improved AmyK38 production, which was associated with alleviation of the secretion stress response. These results suggest that the optimal external pH for the secretion of AmyK38 is higher than the typical external pH of growth medium used to culture B. subtilis. Under controlled pH conditions, the highest production level (1.08 g l(-1)) of AmyK38 was obtained using strain MGB874. CONCLUSIONS: We demonstrated for the first time that RocG is an important factor for secretory enzyme production in B. subtilis through its role in preventing acidification of the growth medium. As expected, a higher external pH enabled a more efficient secretion of the alkaline α-amylase AmyK38 in B. subtilis. Under controlled pH conditions, the reduced-genome strain MGB874 was demonstrated to be a beneficial host for the production of AmyK38.

    DOI PubMed

    Scopus

    13
    Citation
    (Scopus)

  • Expression of a small (p)ppGpp synthetase, YwaC, in the (p)ppGpp(0) mutant of Bacillus subtilis triggers YvyD-dependent dimerization of ribosome.

    Kazumi Tagami, Hideaki Nanamiya, Yuka Kazo, Marie Maehashi, Shota Suzuki, Eri Namba, Masahiro Hoshiya, Ryo Hanai, Yuzuru Tozawa, Takuya Morimoto, Naotake Ogasawara, Yasushi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Masaki Yoshida, Haruko Kuroiwa, Tsuneyoshi Kuroiwa, Yoshiaki Ohashi, Fujio Kawamura

    MicrobiologyOpen   1 ( 2 ) 115 - 34  2012.06  [International journal]

    　View Summary

    To elucidate the biological functions of small (p)ppGpp synthetases YjbM and YwaC of Bacillus subtilis, we constructed RIK1059 and RIK1066 strains carrying isopropyl-β-D-thiogalactopyranoside (IPTG) inducible yjbM and ywaC genes, respectively, in the ΔrelA ΔyjbM ΔywaC triple mutant background. While the uninduced and IPTG-induced RIK1059 cells grew similarly in LB medium, the growth of RIK1066 cells was arrested following the addition of IPTG during the early exponential growth phase. Induction of YwaC expression by IPTG also severely decreased the intracellular GTP level and drastically altered the transcriptional profile in RIK1066 cells. Sucrose density gradient centrifugation analysis of the ribosomal fractions prepared from the IPTG-induced RIK1066 cells revealed three peaks corresponding to 30S, 50S, and 70S ribosome particles, and also an extra peak. Electron microscope studies revealed that the extra peak fraction contained dimers of 70S ribosomes, which were similar to the Escherichia coli 100S ribosomes. Proteomic analysis revealed that the 70S dimer contained an extra protein, YvyD, in addition to those found in the 70S ribosome. Accordingly, strain resulting from the disruption of the yvyD gene in the RIK1066 cells was unable to form 70S dimers following IPTG induction, indicating that YvyD is required for the formation of these dimers in B. subtilis.

    DOI PubMed

    Scopus

    62
    Citation
    (Scopus)

  • Identification and characterization of a novel polysaccharide deacetylase C (PdaC) from Bacillus subtilis.

    Kaori Kobayashi, I Putu Sudiarta, Takeko Kodama, Tatsuya Fukushima, Katsutoshi Ara, Katsuya Ozaki, Junichi Sekiguchi

    The Journal of biological chemistry   287 ( 13 ) 9765 - 9776  2012.03  [International journal]

    　View Summary

    Cell wall metabolism and cell wall modification are very important processes that bacteria use to adjust to various environmental conditions. One of the main modifications is deacetylation of peptidoglycan. The polysaccharide deacetylase homologue, Bacillus subtilis YjeA (renamed PdaC), was characterized and found to be a unique deacetylase. The pdaC deletion mutant was sensitive to lysozyme treatment, indicating that PdaC acts as a deacetylase. The purified recombinant and truncated PdaC from Escherichia coli deacetylated B. subtilis peptidoglycan and its polymer, (-GlcNAc-MurNAc[-L-Ala-D-Glu]-)(n). Surprisingly, RP-HPLC and ESI-MS/MS analyses showed that the enzyme deacetylates N-acetylmuramic acid (MurNAc) not GlcNAc from the polymer. Contrary to Streptococcus pneumoniae PgdA, which shows high amino acid sequence similarity with PdaC and is a zinc-dependent GlcNAc deacetylase toward peptidoglycan, there was less dependence on zinc ion for deacetylation of peptidoglycan by PdaC than other metal ions (Mn(2+), Mg(2+), Ca(2+)). The kinetic values of the activity toward B. subtilis peptidoglycan were K(m) = 4.8 mM and k(cat) = 0.32 s(-1). PdaC also deacetylated N-acetylglucosamine (GlcNAc) oligomers with a K(m) = 12.3 mM and k(cat) = 0.24 s(-1) toward GlcNAc(4). Therefore, PdaC has GlcNAc deacetylase activity toward GlcNAc oligomers and MurNAc deacetylase activity toward B. subtilis peptidoglycan.

    DOI PubMed

    Scopus

    40
    Citation
    (Scopus)

  • Combined effect of improved cell yield and increased specific productivity enhances recombinant enzyme production in genome-reduced Bacillus subtilis strain MGB874.

    Kenji Manabe, Yasushi Kageyama, Takuya Morimoto, Tadahiro Ozawa, Kazuhisa Sawada, Keiji Endo, Masatoshi Tohata, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    Applied and environmental microbiology   77 ( 23 ) 8370 - 81  2011.12  [International journal]

    　View Summary

    Genome reduction strategies to create genetically improved cellular biosynthesis machineries for proteins and other products have been pursued by use of a wide range of bacteria. We reported previously that the novel Bacillus subtilis strain MGB874, which was derived from strain 168 and has a total genomic deletion of 874 kb (20.7%), exhibits enhanced production of recombinant enzymes. However, it was not clear how the genomic reduction resulted in elevated enzyme production. Here we report that deletion of the rocDEF-rocR region, which is involved in arginine degradation, contributes to enhanced enzyme production in strain MGB874. Deletion of the rocDEF-rocR region caused drastic changes in glutamate metabolism, leading to improved cell yields with maintenance of enzyme productivity. Notably, the specific enzyme productivity was higher in the reduced-genome strain, with or without the rocDEF-rocR region, than in wild-type strain 168. The high specific productivity in strain MGB874 is likely attributable to the higher expression levels of the target gene resulting from an increased promoter activity and plasmid copy number. Thus, the combined effects of the improved cell yield by deletion of the rocDEF-rocR region and the increased specific productivity by deletion of another gene(s) or the genomic reduction itself enhanced the production of recombinant enzymes in MGB874. Our findings represent a good starting point for the further improvement of B. subtilis reduced-genome strains as cell factories for the production of heterologous enzymes.

    DOI PubMed

    Scopus

    67
    Citation
    (Scopus)

  • Secretion of biologically-active human interferon-β by Bacillus subtilis.

    Hiroshi Kakeshita, Yasushi Kageyama, Keiji Endo, Masatoshi Tohata, Katsutoshi Ara, Katsuya Ozaki, Kouji Nakamura

    Biotechnology letters   33 ( 9 ) 1847 - 52  2011.09  [International journal]

    　View Summary

    Human interferon-β (hIFN-β) was used as a heterologous model protein to investigate the effects of the Bacillus subtilis AmyE propeptide and co-expression of PrsA in enhancing the secretion of heterologous proteins in B. subtilis. Secretion and activity of hIFN-β with AmyE propeptide increased by more than four-fold compared to that without AmyE propeptide. Moreover, under conditions of co-expressed PrsA, the secretion production and activity of hIFN-β with AmyE propeptide increased by more than 1.5-fold. AmyE propeptide and co-expression of PrsA thus have an additive effect on enhancing the production of the hIFN-β in B. subtilis.

    DOI PubMed

    Scopus

    19
    Citation
    (Scopus)

  • Propeptide of Bacillus subtilis amylase enhances extracellular production of human interferon-α in Bacillus subtilis.

    Hiroshi Kakeshita, Yasushi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Kouji Nakamura

    Applied microbiology and biotechnology   89 ( 5 ) 1509 - 17  2011.03  [International journal]

    　View Summary

    The Gram-positive bacterium, Bacillus subtilis and related species are widely used industrially as hosts for producing enzymes. These species possess a high potential to produce secreted proteins into the culture medium. Nevertheless, the secretion of heterologous proteins by these species is frequently inefficient. In this study, the human interferon-α2b (hIFN-α2b) was used as a heterologous model protein, to investigate the effect of B. subtilis AmyE propeptide in enhancing the secretion of heterologous proteins in B. subtilis. We found that the secretion production and activity of hIFN-α2b with AmyE propeptide increased by more than threefold, compared to that without AmyE propeptide. The maximum amount of secreted hIFN-α2b with propeptide was 14.8 ± 0.6 μg ml⁻¹. In addition, the pro-hIFN-α2b bioactivity reached 5.4 ± 0.5 x 10⁷ U mg⁻¹, which is roughly the same level as that of the non-propeptide hIFN-α2b. These results indicated that AmyE propeptide enhanced the secretion of the hIFN-α2b protein from B. subtilis. This study provides a useful method to enhance the extracellular production of heterologous proteins in B. subtilis.

    DOI PubMed

    Scopus

    10
    Citation
    (Scopus)

  • A novel small protein of Bacillus subtilis involved in spore germination and spore coat assembly.

    Takeko Kodama, Takeshi Matsubayashi, Tadayoshi Yanagihara, Hiroyuki Komoto, Katsutoshi Ara, Katsuya Ozaki, Ritsuko Kuwana, Daisuke Imamura, Hiromu Takamatsu, Kazuhito Watabe, Junichi Sekiguchi

    Bioscience, biotechnology, and biochemistry   75 ( 6 ) 1119 - 28  2011  [International journal]

    　View Summary

    Two small genes named sscA (previously yhzE) and orf-62, located in the prsA-yhaK intergenic region of the Bacillus subtilis genome, were transcribed by SigK and GerE in the mother cells during the later stages of sporulation. The SscA-FLAG fusion protein was produced from T(5) of sporulation and incorporated into mature spores. sscA mutant spores exhibited poor germination, and Tricine-SDS-PAGE analysis showed that the coat protein profile of the mutant differed from that of the wild type. Bands corresponding to proteins at 59, 36, 5, and 3 kDa were reduced in the sscA null mutant. Western blot analysis of anti-CotB and anti-CotG antibodies showed reductions of the proteins at 59 kDa and 36 kDa in the sscA mutant spores. These proteins correspond to CotB and CotG. By immunoblot analysis of an anti-CotH antibody, we also observed that CotH was markedly reduced in the sscA mutant spores. It appears that SscA is a novel spore protein involved in the assembly of several components of the spore coat, including CotB, CotG, and CotH, and is associated with spore germination.

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  • A simple method for introducing marker-free deletions in the Bacillus subtilis genome.

    Takuya Morimoto, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    Methods in molecular biology (Clifton, N.J.)   765   345 - 58  2011  [International journal]

    　View Summary

    A genetic tool for introducing marker-free deletions is essential for multiple manipulations of genomes. We have developed a simple and efficient method for creating marker-free deletion mutants of Bacillus subtilis through transformation with recombinant PCR products, using the Escherichia coli mazF gene encoding an endoribonuclease that cleaves free mRNAs as a counterselection tool.

    DOI PubMed

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    11
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  • Dimerization of ribosome was induced by treatment with various stresses in Bacillus subtilis

    Masahiro Hoshiya, Tetsuya Wada, Shota Suzuki, Yasusi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Fujio Kawamura

    GENES & GENETIC SYSTEMS   85 ( 6 ) 421 - 421  2010.12

  • Functional analyses of dimer ribosome and yvyD gene during stationary growth phase in Bacillus subtilis

    Yuka Kazo, Marie Maehashi, Yasusi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Fujio Kawamura

    GENES & GENETIC SYSTEMS   85 ( 6 ) 421 - 421  2010.12

  • Dimerization of ribosomes in sporulating cells in Bacillus subtilis

    Marie Maehashi, Yuka Kazo, Yasushi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Fujio Kawamura

    GENES & GENETIC SYSTEMS   85 ( 6 ) 421 - 421  2010.12

  • Erratum: Enhanced extracellular production of heterologous proteins in bacillus subtilis by deleting the c-terminal region of the SecA secretory machinery (Molecular Biotechnology DOI: 10.1007/s12033-010-9295-0)

    Hiroshi Kakeshita, Yasushi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Kouji Nakamura

    Molecular Biotechnology   46 ( 3 ) 320  2010.11

    DOI

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  • Enhanced extracellular production of heterologous proteins in Bacillus subtilis by deleting the C-terminal region of the SecA secretory machinery.

    Hiroshi Kakeshita, Yasushi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Kouji Nakamura

    Molecular biotechnology   46 ( 3 ) 250 - 7  2010.11  [International journal]

    　View Summary

    In this study, we examined the effects of modifying the C-terminal region of the SecA protein on the production of heterologous proteins in Bacillus subtilis. SecA was selected as a candidate among the components of the Sec system due to its ability to interact directly with both the precursors and membrane translocases. A phylogenetic comparison demonstrated that the C-terminal region is not well conserved among eubacterial SecA proteins. The deletion of the 61 amino acids at the C-terminal region led to an 83% increase in extracellular alkaliphilic Bacillus sp. thermostable alkaline cellulase (Egl-237) activity. Moreover, the productivity of human interferon α (hIFN-α2b) was increased by 2.2-fold compared to the wild-type SecA, by deletion of these 61 amino acids. We indicated that the deletion of the C-terminal domain (CTD) of SecA enhanced the secretion of two different heterologous protein, Egl-237 and hIFN-α2b. This study provides a useful method to enhance the extracellular production of heterologous proteins in B. subtilis.

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  • Functional analysis of a novel ppGpp synthetase, YwaC, and regulatory mechanism for the dimerization of ribosome, in Bacillus subtilis

    Kazumi Tagami, Kenta Masuda, Marie Maehashi, Yoshitaka Hirohata, Masaki Yoshida, Haruko Kuroiwa, Tsuneyoshi Kuroiwa, Hideaki Nanamiya, Yuzuru Tozawa, Shenghao Liu, Yasushi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Fujio Kawamura

    GENES & GENETIC SYSTEMS   84 ( 6 ) 455 - 455  2009.12

  • A new simple method to introduce marker-free deletions in the Bacillus subtilis genome.

    Takuya Morimoto, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    Genes & genetic systems   84 ( 4 ) 315 - 8  2009.08  [Domestic journal]

    　View Summary

    A genetic tool to introduce marker-free deletions is essential for multiple manipulations of genomes. We report a simple and efficient method to create marker-free deletion mutants of Bacillus subtilis through transformation with recombinant PCR products, using the Escherichia coli mazF gene encoding an endoribonuclease that cleaves free mRNAs as a counter-selection tool. Our method will be applicable to any bacterium in which introduction of the mazF cassette into the genome by double crossover homologous recombination is possible.

    DOI PubMed

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    39
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  • Genome reduction in Bacillus subtilis and enhanced productivities of recombinant proteins

    Yasushi Kageyama, Takuya Morimoto, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    Bacterial DNA, DNA Polymerase and DNA Helicases     119 - 136  2009

    　View Summary

    Bacillus subtilis, which is one of the most important host microorganisms for largescale industrial production of useful proteins, has a genome of 4.2 Mb with approximately 4106 protein-coding genes. Some of these genes are expected to be unnecessary for industrial production of proteins under controlled conditions and may be wasteful with regard to energy consumption. We attempted to reduce the genome size of B. subtilis by deleting unnecessary regions of the genome to allow the construction of simplified host cells as a platform for the further development of novel genetic systems with increased productivity. First, we generated the strain MGB469 with deletion of all prophage (SPβ and PBSX) and prophage-like (pro1-7 and skin) sequences, with the exception of pro7, as well as two large operons that produce secondary metabolites (pks and pps). These cells showed normal growth, but no beneficial effects were observed with regard to recombinant protein production from plasmids carrying the corresponding genes. Second, we constructed several multiple-deletion mutants containing additional deletions in the MGB469 genome, resulting in total genome size reductions of 0.78 to 0.99 Mb. In most of the multiple-deletion series, extensive deletion mutants showed no beneficial improvements in traits as host strains. The strain MG1M with a total genome size reduction of 0.99 Mb showed unstable phenotypes with regard to growth rate, cell morphology, and recombinant protein productivity after successive culture, making it inappropriate for further studies. In addition, strain MGB943 derived from another lineage with genome reduction of 0.94 Mb showed reduced recombinant cellulase productivity. Finally, we generated another multiple-deletion series including the mutant MGB874 with a total genome deletion of 0.87 Mb. In comparison to wild-type cells, the metabolic network of the mutant strain was reorganized after entry into the transition state due to the synergistic effects of multiple deletions. Moreover, the levels of production of extracellular cellulase and protease from transformed plasmids carrying the corresponding genes were markedly increased. Our results demonstrated the effectiveness of a synthetic genomic approach with reduction of genome size to generate novel and useful bacteria for industrial uses. © 2010 by Nova Science Publishers, Inc. All rights reserved.

  • Introduction of marker-free deletions in Bacillus subtilis using the AraR repressor and the ara promoter.

    Shenghao Liu, Keiji Endo, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    Microbiology (Reading, England)   154 ( Pt 9 ) 2562 - 2570  2008.09  [International journal]

    　View Summary

    We have developed a system for the induction of marker-free mutation of Bacillus subtilis. The system features both the advantages of the use of antibiotic-resistance markers for mutant selection, and the ability to efficiently remove the markers, leaving unmarked mutations in the genome. It utilizes both a selective marker cassette and a counter-selective marker cassette. The selective marker cassette contains a chloramphenicol-resistance gene and the araR gene, which encodes the repressor for the arabinose operon (ara) of B. subtilis. The counter-selective marker cassette consists of a promoterless neomycin (Nm)-resistance gene (neo) fused to the ara promoter. First, the chromosomal araR locus is replaced with the counter-selective marker cassette by double-crossover homologous recombination and positive selection for Nm resistance. The selective marker cassette is connected with upstream and downstream sequences from the target locus, and is integrated into the upstream region of the target locus by a double-crossover event. This integration is also positively selected for, using chloramphenicol resistance. In the resultant strain, AraR, encoded by araR on the selective marker cassette, represses the expression of neo in the absence of l-arabinose. Finally, the eviction of the selective marker cassette together with the target locus is achieved by an intra-genomic single-crossover event between the two downstream regions of the target locus, and can be selected for based on Nm resistance, because of the excision of araR. The counter-selective marker cassette remaining in the genome, whose expression is switched on or off based on the excision or introduction of the selective marker cassette, is used again for the next round of deletion. Using this system, the 3.8 kb iolS-csbC region and the 41.8 kb hutM-csbC region have been efficiently and successfully deleted, without leaving markers in the target loci. The positive selection and simple procedure will make it a useful tool for the construction of multiple mutations.

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  • Enhanced recombinant protein productivity by genome reduction in Bacillus subtilis.

    Takuya Morimoto, Ryosuke Kadoya, Keiji Endo, Masatoshi Tohata, Kazuhisa Sawada, Shengao Liu, Tadahiro Ozawa, Takeko Kodama, Hiroshi Kakeshita, Yasushi Kageyama, Kenji Manabe, Shigehiko Kanaya, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    DNA research : an international journal for rapid publication of reports on genes and genomes   15 ( 2 ) 73 - 81  2008.04  [International journal]

    　View Summary

    The emerging field of synthetic genomics is expected to facilitate the generation of microorganisms with the potential to achieve a sustainable society. One approach towards this goal is the reduction of microbial genomes by rationally designed deletions to create simplified cells with predictable behavior that act as a platform to build in various genetic systems for specific purposes. We report a novel Bacillus subtilis strain, MBG874, depleted of 874 kb (20%) of the genomic sequence. When compared with wild-type cells, the regulatory network of gene expression of the mutant strain is reorganized after entry into the transition state due to the synergistic effect of multiple deletions, and productivity of extracellular cellulase and protease from transformed plasmids harboring the corresponding genes is remarkably enhanced. To our knowledge, this is the first report demonstrating that genome reduction actually contributes to the creation of bacterial cells with a practical application in industry. Further systematic analysis of changes in the transcriptional regulatory network of MGB874 cells in relation to protein productivity should facilitate the generation of improved B. subtilis cells as hosts of industrial protein production.

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    124
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  • Bacillus subtilis AprX involved in degradation of a heterologous protein during the late stationary growth phase.

    Takeko Kodama, Keiji Endo, Kazuhisa Sawada, Katsutoshi Ara, Katsuya Ozaki, Hiroshi Kakeshita, Kunio Yamane, Junichi Sekiguchi

    Journal of bioscience and bioengineering   104 ( 2 ) 135 - 43  2007.08  [Domestic journal]

    　View Summary

    In Bacillus subtilis, extracellular protease-deficient mutants have been used in attempts to increase the productivity of heterologous proteins. We detected protease activity of AprX using protease zymography in the culture medium at the late stationary growth phase. An alpha-amylase-A522-PreS2 hybrid protein, in which the PreS2 antigen of human hepatitis B virus (HBV) is fused with the N-terminal 522-amino-acid polypeptide of B. subtilis alpha-amylase, has been produced in multiple-protease-deficient mutants. The B. subtilis KA8AX strain, which is deficient in eight extracellular proteases and AprX, did not show the proteolysis of alpha-amylase-A522-PreS2 in the late stationary growth phase. Moreover, the production of alpha-amylase-A522-PreS2 was about 80 mg/l, which was eight times higher than that by the KA8AX strain previously reported. In addition, we showed the degradation of the heterologous protein by AprX that leaked to the culture medium (probably caused by cell lysis) during the late stationary growth phase.

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  • Bacillus minimum genome factory: effective utilization of microbial genome information.

    Katsutoshi Ara, Katsuya Ozaki, Kouji Nakamura, Kunio Yamane, Junichi Sekiguchi, Naotake Ogasawara

    Biotechnology and applied biochemistry   46 ( Pt 3 ) 169 - 78  2007.03  [International journal]

    　View Summary

    In 1997, the complete genomic DNA sequence of Bacillus subtilis (4.2 Mbp) was determined and 4100 genes were identified [Kunst, Ogasawara, Moszer, Albertini, Alloni, Azevedo, Bertero, Bessieres, Bolotin, Borchert, S. et al. (1997) Nature 90, 249-256]. In addition, B. subtilis, which shows an excellent ability to secrete proteins (enzymes) and antibiotics in large quantities outside the cell, plays an important role in industrial and medical fields. It is necessary to clarify the genes involved in the production of compounds by understanding the network of these 4100 genes and the proceeding analysis of genes of unknown functions. In promoting such a study, it is expected that the regulatory system of B. subtilis can be simplified by the creation of a Bacillus strain with a reduced genome by discriminating genes unnecessary for the production of proteins from essential genes, and deleting as many of these unnecessary genes as possible, which may help to understand this complex network of genes. We have previously distinguished essential and non-essential genes by evaluating the growth and enzyme-producing properties of strains of B. subtilis in which about 3000 genes (except 271 essential genes) have been disrupted or deleted singly, and have successfully utilized the findings from these studies in creating the MG1M strain with an approx. 1 Mbp deletion by serially deleting 17 unnecessary regions from the genome. This strain showed slightly reduced growth in enzyme-production medium, but no marked morphological changes. Moreover, we confirmed that the MG1M strain had cellulase and protease productivity comparable with that of the B. subtilis 168 strain, thus demonstrating that genome reduction does not contribute to a negative influence on enzyme productivity.

    PubMed

  • The accurate replacement of long genome region more than several hundreds kilobases in Bacillus subtilis.

    Shenghao Liu, Keiji Endo, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara

    Genes & genetic systems   82 ( 1 ) 9 - 19  2007.02  [Domestic journal]

    　View Summary

    Competent cell transformation with DNA obtained by the gentle lysis of protoplasts (LP transformation) was used to replace a large genomic region in this study. Discontinuity was detected in the replacement of the donor region tested, probably due to multiple crossover events involving a single donor genome fragment. To overcome discontinuous replacement, we inverted the genomic region to be replaced in the donor used for LP transformation. The replaced region in the transformant was identified to have a continuous genomic region originating from the donor genome. Furthermore, the genome region to be replaced was inverted in the recipient, and the same region and the flanking 10 kb region of both ends was inverted in the donor genome. LP transformation was conducted with the two inversion mutants and it is possible to restrict homologous recombination to the 10 kb flanking regions. Using this method, the 99 kb yxjG-yxbA region, the 249 kb pbpG-yxbA region and the 602 kb yvfT-yxbA region were suggested to be replaced continuously and accurately.

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  • Effect of Bacillus subtilis spo0A mutation on cell wall lytic enzymes and extracellular proteases, and prevention of cell lysis.

    Takeko Kodama, Keiji Endo, Katsutoshi Ara, Katsuya Ozaki, Hiroshi Kakeshita, Kunio Yamane, Junichi Sekiguchi

    Journal of bioscience and bioengineering   103 ( 1 ) 13 - 21  2007.01  [Domestic journal]

    　View Summary

    The Bacillus subtilis spo0A mutant is an adequate host for extracellular protein production (e.g., alpha-amylase). However the mutant was prone to cell lysis. SDS-PAGE and zymography of cell wall lytic proteins indicated that the spo0A mutant contained high amounts of two major autolysins (LytC [CwlB] and LytD [CwlG]) and two minor cell wall lytic enzymes (LytE [CwlF] and LytF [CwlE]). On the other hand, the expression of eight extracellular protease genes was very poor or absent in the spo0A mutant. An eight-extracellular-protease-deficient mutant (Dpr8 strain) was constructed and the strain also exhibited cell lysis. The autolysins from the spo0A mutant were degraded by the supernatant of the wild type but not degraded by that of the Dpr8 mutant. These results suggest that the extensive cell lysis of the spo0A mutant was partially caused by the stability of autolysins via the decrease of the extracellular proteases. The introduction of a major autolysin and/or SigD mutations into the spo0A mutant was effective for preventing cell lysis.

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  • Extracellular production of human cystatin S and cystatin SA by Bacillus subtilis.

    Shunichi Akiba, Yasuhiro Hayashi, Yoshihiro Hakamada, Keiji Endo, Katsutoshi Ara, Shuji Kawai, Eiichi Saitoh

    Protein expression and purification   49 ( 2 ) 203 - 10  2006.10  [International journal]

    　View Summary

    We herein describe the development of a Bacillus subtilis system that can be used to produce large quantities of recombinant (r-) human salivary cystatins, a cysteine protease inhibitor of family 2 in the cystatin superfamily. The B. subtilis that lacked the alkaline protease E gene (DeltaaprE type mutant strain) was prepared by homologous recombination. The cDNA fragments coding for mature cystatins (S and SA) were ligated in frame to the DNA segment for the signal peptide of endoglucanase in the pHSP-US plasmid vector that was then use to transform the DeltaaprE type mutant strain of B. subtilis. The transformants carrying the expression vectors were cultivated in 5-L jar fermenters for 3 days at 30 degrees C. Both r-cystatin S and r-cystatin SA were successfully expressed and secreted into the culture broth, and were purified using a fast performance liquid chromatography system. The first use of DeltaaprE type mutant strain of B. subtilis made it possible to obtain a high yield of secreted protein, which makes this system an improvement over expression in Escherichia coli. We conclude that this system has high utility for expression of commercial quantities of secreted proteins.

    PubMed

  • Foot odor due to microbial metabolism and its control.

    Katsutoshi Ara, Masakatsu Hama, Syunichi Akiba, Kenzo Koike, Koichi Okisaka, Toyoki Hagura, Tetsuro Kamiya, Fusao Tomita

    Canadian journal of microbiology   52 ( 4 ) 357 - 64  2006.04  [International journal]

    　View Summary

    To characterize foot odor, we analyzed its components by sensory tests, isolated microorganisms that produce it, and evaluated the mechanism of the occurrence of foot odor. As a result, foot odor was found to be derived from isovaleric acid, which is produced when Staphylococcus epidermidis, a resident species of the normal cutaneous microbial flora, degrades leucine present in sweat. In addition, Bacillus subtilis was detected in the plantar skin of subjects with strong foot odor, and this species was shown to be closely associated with increased foot odor. Therefore, we screened various naturally occurring substances and fragrant agents that inhibit microbial production of foot odor without disturbing the normal microbial flora of the human skin. As a result, we identified citral, citronellal, and geraniol as fragrant agents that inhibit the generation of isovaleric acid at low concentrations.

    PubMed

  • Survey of fungal contamination in ordinary houses in Japan

    Katsutoshi Ara, Maki Aihara, Miyuki Ojima, Yasuhiko Toshima, Chiaki Yabune, Hajime Tokuda, Syuji Kawai, Nobuo Ueda, Tatsuaki Tanaka, Kazuo Akiyama, Kosuke Takatori

    Allergology International   53 ( 4 ) 369 - 377  2004

    　View Summary

    Background: Because fungi in the indoor environment strongly affect not only damage to and the deterioration of building materials, but also affect human health, it is important to know the distribution of fungi within an indoor environment. Therefore, in the present study, we examined fungi in houses over a period of 1 year and attempted to produce an indoor fungal contamination map for Japanese houses.<br> Methods: Fungi were collected at approximately 100 fixed points in 81 ordinary houses around the Kanto District using either the stamp or dressing tape methods between 1999 and 2000. A commercially available potato dextrose agar culture medium was used to incubate the fungi collected. After incubation, fungi were quantified and identified by routine methods and the fungal conditions in the indoor environment was evaluated.<br> Results: The relationships between the fungal conditions in the indoor environment found around the Kanto District and parameters such as the season, area in the house and indoor environment were analyzed. According to the fungal flora found in the present study, the indoor environment in Japanese homes was classified into three areas: (i) relatively wet areas, such as the bathroom, lavatory and kitchen, where hygrophilic fungi and yeasts are often detected; (ii) relatively dry areas, such as the living room and Japanese-style rooms, where xerophilic fungi are often detected; and (iii) areas where wet and dry parts coexist, such as bedrooms and closets containing futons and clothes with moisture, where both hydrophilic and xerophilic fungi, as well as yeasts, are detected. In the presnt survey, seasonal changes in the fungi detected in the indoor environment were small.<br> Conclusions: We confirmed the actual fungal conditions in the indoor environment and produced a fungal map.<br>

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  • Hygiene measures considering actual distributions of microorganisms in Japanese households

    M. Ojima, Y. Toshima, E. Koya, K. Ara, H. Tokuda, S. Kawai, F. Kasuga, N. Ueda

    Journal of Applied Microbiology   93 ( 5 ) 800 - 809  2002.11

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  • Bacterial contamination of Japanese households and related concern about sanitation

    M. Ojima, Y. Toshima, E. Koya, K. Ara, S. Kawai, N. Ueda

    International Journal of Environmental Health Research   12 ( 1 ) 41 - 52  2002.03

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  • Effect of Spore-bearing Lactic Acid-forming Bacteria ( Bacillus coagulans SANK 70258) Administration on the Intestinal Environment, Defecation Frequency, Fecal Characteristics and Dermal Characteristics in Humans and Rats

    Katsutoshi Ara, Shinichi Meguro, Tadasi Hase, Ichirou Tokimitsu, Kazuya Otsuji, Shuji Kawai, Susumu Ito, Hisakazu Iino

    Microbial Ecology in Health and Disease   14 ( 1 ) 4 - 13  2002.01

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  • Production of Isopropylcis-6-Hexadecenoate by Regiospecific Desaturation of Isopropyl Palmitate by a Double Mutant of aRhodococcusStrain

    Kenzo KOIKE, Mikio TAKAIWA, Katsutoshi ARA, Shigeo INOUE, Yoshiharu KIMURA, Susumu ITO

    Bioscience, Biotechnology, and Biochemistry   64 ( 2 ) 399 - 404  2000.01

    　View Summary

    Resting cells of a double mutant noted as KSM-MT66,derived from Rhodococcus sp. strain KSM-B-3 by UV irradiation, were found to cis-desaturate isopropyl hexadecanoate, yielding isopropyl cis-6-hex-adecenoate. Addition of sodium glutamate (1.0%), Mg SO_4 (2 mM), and thiamine (2 mM) increased the productivity of the unsaturated product in phosphate buffer. Optimal temperature and pH for the reaction were around 26℃ and 7,respectively. Under the optimized conditions, more than 50 g/I of isopropyl cis-6-hexadecenoate was produced after a 3-day incubation by resting cells of the mutant. Thus, cis-6-hexadecenoic acid, the main component of human sebaceous lipids, can be manufactured economically by the rhodococcal bioconversion.

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  • Regiospecific Internal Desaturation of Aliphatic Compounds by a Mutant Rhodococcus Strain

    Kenzo Koike, Katsutoshi Ara, Shigehito Adachi, Hirofumi Takigawa, Hajime Mori, Shigeo Inoue, Yoshiharu Kimura, Susumu Ito

    Applied and Environmental Microbiology   65 ( 12 ) 5636 - 5638  1999.12

    　View Summary

    ABSTRACT

    A mutant Rhodococcus strain lacking the ability to utilize 1-chlorohexadecane was found to cis -desaturate aliphatic compounds, such as 1-chlorohexadecane, n -hexadecane, and heptadecanonitrile, yielding corresponding products with a double bond mainly at the ninth carbon from the terminal methyl groups. A new oxidative pathway involving the cis -desaturation step was suggested for alkane utilization by Rhodococcus spp.

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  • Enzymatic Properties of a Novel Liquefying α-Amylase from an Alkaliphilic Bacillus Isolate and Entire Nucleotide and Amino Acid Sequences

    Kazuaki Igarashi, Yuji Hatada, Hiroshi Hagihara, Katsuhisa Saeki, Mikio Takaiwa, Takaaki Uemura, Katsutoshi Ara, Katsuya Ozaki, Shuji Kawai, Tohru Kobayashi, Susumu Ito

    Applied and Environmental Microbiology   64 ( 9 ) 3282 - 3289  1998.09

    　View Summary

    ABSTRACT

    A novel liquefying α-amylase (LAMY) was found in cultures of an alkaliphilic Bacillus isolate, KSM-1378. The specific activity of purified LAMY was approximately 5,000 U mg of protein −1 , a value two- to fivefold greater between pH 5 and 10 than that of an industrial, thermostable Bacillus licheniformis enzyme. The enzyme had a pH optimum of 8.0 to 8.5 and displayed maximum activity at 55°C. The molecular mass deduced from sodium dodecyl sulfate-polyacrylamide gel electrophoresis was approximately 53 kDa, and the apparent isoelectric point was around pH 9. This enzyme efficiently hydrolyzed various carbohydrates to yield maltotriose, maltopentaose, maltohexaose, and maltose as major end products after completion of the reaction. Maltooligosaccharides in the maltose-to-maltopentaose range were unhydrolyzable by the enzyme. The structural gene for LAMY contained a single open reading frame 1,548 bp in length, corresponding to 516 amino acids that included a signal peptide of 31 amino acids. The calculated molecular mass of the extracellular mature enzyme was 55,391 Da. LAMY exhibited relatively low amino acid identity to other liquefying amylases, such as the enzymes from B. licheniformis (68.9%), Bacillus amyloliquefaciens (66.7%), and Bacillus stearothermophilus (68.6%). The four conserved regions, designated I, II, III, and IV, and the putative catalytic triad were found in the deduced amino acid sequence of LAMY. Essentially, the sequence of LAMY was consistent with the tertiary structures of reported amylolytic enzymes, which are composed of domains A, B, and C and which include the well-known (α/β) 8 barrel motif in domain A.

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  • Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures

    S. Ito, Tohru Kobayashi, Katsutoshi Ara, Katsuya Ozaki, Shuji Kawai, Yuji Hatada

    Extremophiles   2 ( 3 ) 185 - 190  1998.08

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  • Amino Acid Sequence and Molecular Structure of an Alkaline Amylopullulanase from Bacillus That Hydrolyzes α-1,4 and α-1,6 Linkages in Polysaccharides at Different Active Sites

    Yuji Hatada, Kazuaki Igarashi, Katsuya Ozaki, Katsutoshi Ara, Jun Hitomi, Tohru Kobayashi, Shuji Kawai, Tomoyoshi Watabe, Susumu Ito

    Journal of Biological Chemistry   271 ( 39 ) 24075 - 24083  1996.09

    DOI

  • Separation of Functional Domains for theα-1,4 andα-1,6 Hydrolytic Activities of aBacillusAmylopullulanase by Limited Proteolysis with Papain

    Katsutoshi Ara, Kazuaki Igarashi, Hiroshi Hagihara, Kazuhisa Sawada, Tohru Kobayashi, Susumu Ito

    Bioscience, Biotechnology, and Biochemistry   60 ( 4 ) 634 - 639  1996.01

    　View Summary

    An amylopullulanase (APase) from alkalophilic Bacillus sp. KSM-1378 hydrolyzes both α-1,6 linkages in pullulan and α-1,4 linkages in other polysaccharides, each being maximally active at an alkaline pH, to generate oligosaccharides. We analyzed proteolytic fragments that were produced by exposing pure APase to various proteases, to identify its catalytic domain(s). The intact, pure 210-kDa APase was partially digested with papain for a short time, yielding simultaneously two smaller non-overlapping active fragments, designated amylose-hydrolyzing fragment (AHF114, 114kDa) and pullulan-hydrolyzing fragment (PHF102,102kDa). The two truncated protein fragments, each containing a single catalytic domain, were purified to homogeneity. The purified AHF114 and PHF102 had similar enzymatic properties to the amylase and pullulanase activities, respectively, of intact APase. The partial amino-terminal sequences of APase and AHF114 were both Glu-Thr-Gly-Asp-Lys-Arg-Ile-Glu-Phe-Ser-Tyr-Glu-Arg-Pro and that of PHF102 was Thr-Val-Pro-Leu-Ala-Leu-Val-Ser-Gly-Glu-Val-Leu-Ser-Asp-Lys-Leu. These results were direct evidence that the α-1,6 and α-1,4 hydrolytic activities were associated with two different active sites in this novel enzyme. Our alkaline APase is obviously a "biheaded enzyme".

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    Citation
    (Scopus)

  • Purification and characterization of an alkaline amylopullulanase with both α-1,4 and α-1,6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378

    Katsutoshi Ara, Katsuhisa Saeki, Kazuaki Igarashi, Mikio Takaiwa, Takaaki Uemura, Hiroshi Hagihara, Shuji Kawai, Susumu Ito

    Biochimica et Biophysica Acta (BBA) - General Subjects   1243 ( 3 ) 315 - 324  1995.04

    DOI

  • An Alkaline Amylopullulanase from AlkalophilicBacillussp. KSM-1378; Kinetic Evidence for Two Independent Active Sites for theα-1,4 andα-1,6 Hydrolytic Reactions

    Katsutoshi Ara, Kazuaki Igarashi, Katsuhisa Saeki, Susumu Ito

    Bioscience, Biotechnology, and Biochemistry   59 ( 4 ) 662 - 666  1995.01

    　View Summary

    Alkalophilic Bacillus sp. KSM-1378 produces an alkaline amylopullulanase that hydrolyzes both α-1, 4 linkages in amylose, amylopectin, and glycogen and α-1, 6 linkages in pullulan. The hydrolytic activities against amylose and pullulan were specifically inhibited by maltotriose (K_i=0. 5mM), isomaltitol (K_i=5. 2mM), and methyl α-D-galactoside (K_i=40mM) and by β-cyclodextrin (K_i=0. 9mM), α-cyclodextrin (K_i=11mM), and raffinose (K_i=31mM), respectively, in a competitive manner in each case. Inhibition by N-bromosuccinimide of the α-amylase activity was prevented by amylose but not by pullulan, while inhibition by N-bromosuccinimide of the pullulanase activity was prevented by pullulan but not by amylose. Kinetics of reactions in the simultaneous presence of amylose and pullulan indicated that the observed rates of formation of products closely matched those predicted by a kientic model in which the α-1, 4 and α-1, 6 hydrolytic reactions were catalyzed at two independent active sites. Incubation of the enzyme at 40℃ and pH 9. 0 caused complete inactivation of the amylase activity within 4 days, but the pullulanase activity remained at the original level under the same conditions. This alkaline amylopullulanase can, therefore, be considered to be a "two-headed" enzyme molecule.

    DOI CiNii

    Scopus

    28
    Citation
    (Scopus)

  • Purification and characterization of an alkaline isoamylase from an alkalophilic strain of Bacillus

    K. Ara, K. Saeki, S. Ito

    Journal of General Microbiology   139 ( 4 ) 781 - 786  1993.04

    DOI

    Scopus

    34
    Citation
    (Scopus)

  • Nucleotide Sequence of the Gene That Encodes a Neopullulanase from an AlkalophilicBacillus

    Kazuaki Igarashi, Katsutoshi Ara, Katsuhisa Saeki, Katsuya Ozaki, Shuji Kawai, Susumu Ito

    Bioscience, Biotechnology, and Biochemistry   56 ( 3 ) 514 - 516  1992.01

    DOI CiNii

    Scopus

    49
    Citation
    (Scopus)

  • Purification and Some Properties of an Alkaline Pullulanase from AlkalophilicBacillussp. KSM-1876

    Katsutoshi Ara, Kazuaki Igarashi, Katsuhisa Saeki, Shuji Kawai, Susumu Ito

    Bioscience, Biotechnology, and Biochemistry   56 ( 1 ) 62 - 65  1992.01

    　View Summary

    A novel alkaline pullulanase (pullulan 6-glucanohydrolase, EC3.2.1.41) was purified to homogeneity from the culture filtrate of the alkalophilic Bacillus sp.KSM-1876. The pullulanase had an optimum pH for activity of around 10.0-10.5,which is the highest pH for optimum activity of any pullulanases reported to date. The optimum temperature at pH 10 was around 50℃. The enzyme had a molecular mass of 120 kDa and an isoelectric point of pH 5.2. The enzyme acted specifically on pullulan to generate maltotriose as the major end product ; the K_m for pullulan was 1.8mg/ml. N-Bromosuccinimide abolished the enzymatic activity, and pullulan protected the enzyme from inactivation by this tryptophan-specific oxidant, suggesting that a tryptophan residue (s) is involved in the mechanism of action of the pullulanase from Bacillus sp.KSM-1876.

    DOI CiNii

    Scopus

    47
    Citation
    (Scopus)

  • Neutrophilic Bacillus strain, KSM-522, that produces an alkaline carboxymethyl cellulase.

    Shuji KAWAI, Hiromi OKOSHI, Katsuya OZAKI, Shitsuw SHQCATA, Katsutoshi ARA, Susumu ITO

    Agricultural and Biological Chemistry   52 ( 6 ) 1425 - 1431  1988

    　View Summary

    A strain of Bacillus that produced an alkaline carboxymethyl cellulase (CMCase) was isolated from a soil sample and was found to be taxonomically similar to Bacillus pumilus. The growth rate and production of CMCase were greater during cultivation in neutral medium than in alkaline medium. Glucose, sucrose, cellobiose, maltose, starch and xylan, in addition to carboxymethyl cellulose, induced the production of the CMCase. The CMCase, partially purified by precipitation with ammonium sulfate, was very active over the pH range of 7 to 10 and was fairly stable over a broad pH range (pH 5〜12). The reaction catalyzed by the CMCase showed an optimum temperature of about 50℃ and the enzyme was stable at temperatures up to 50℃ or higher at pH 9. The partially purified enzyme preparation exhibited essentially no activity toward insoluble cellulosic materials such as filter paper, Avicel, cellulose powder, or alkali- or H_3PO_4-swollen celluloses, nor was it active toward cellobiose or p-nitrophenyl-β-D-cellobioside. The CMCase activity was characteristically stable in the presence of surfactants, chelating agents and proteolytic enzymes used as components of laundry detergents.

    DOI CiNii

    Scopus

    36
    Citation
    (Scopus)

  • Protocatechuate 3,4-Dioxygenase from Nocardia erythropolis†

    Ryuichiro Kurane, Katsutoshi Ara, Isei Nakamura, Tomoo Suzuki, Seiichi Fukuoka

    Agricultural and Biological Chemistry   48 ( 8 ) 2105 - 2111  1984.08

    DOI

    Scopus

    15
    Citation
    (Scopus)

  • Determination of trace levels of fatty acid metal salts by high-performance liquid chromatography with fluorescence prelabeling

    Katsumi Hayashi, Jiro Kawase, Koichi Yoshimura, Katsutoshi Ara, Kazuro Tsuji

    Analytical Biochemistry   136 ( 2 ) 314 - 320  1984.02

    DOI

    Scopus

    36
    Citation
    (Scopus)

▼display all

Books and Other Publications

  • PMP試験 完全研究 (なるほどナットク!)

    ( Part： Contributor)

    オーム社  2022.03 ISBN: 4274201740

    ASIN

  • 薬膳の知恵 new food industry3

    荒勝俊( Part： Edit, 東洋医学 薬膳)

    荒勝俊（国会図書館所蔵 23554540）  2020

  • Microbial production : from genome design to cell engineering

    穴澤, 秀治, 清水, 昌( Part： Contributor, Ｃreation of Ｎovel Ｔechnologies for Ｅxtracellular Ｐrotein Ｐroduction Ｔoward the Ｄevelopment of Bacillus subtilis Genome Factories)

    Springer  2014.03 ISBN: 9784431546061

    ASIN

  • 合成生物工学の隆起 : 有用物質の新たな生産法構築をめざして

    植田, 充美( Part： Contributor, ミニマムゲノムー枯草菌)

    シーエムシー出版  2012.04 ISBN: 9784781305639

  • バイオマス分解酵素研究の最前線 : セルラーゼ・ヘミセルラーゼを中心として

    近藤, 昭彦, 天野, 良彦, 田丸, 浩( Part： Contributor, Bacillus)

    シーエムシー出版  2012.03 ISBN: 9784781305219

  • Strain Engineering: Methods and Protocols (Methods in Molecular Biology, 765)

    ( Part： Contributor, A Simple Method for Introducing Marker-Free Deletions in the Bacillus subtilis Genome)

    2011.07 ISBN: 9781617791963

  • 薬膳の知恵 new food industry2

    荒勝俊( Part： Edit, 東洋医学 薬膳)

    荒勝俊（国会図書館所蔵 23554538）  2011

  • 薬膳の知恵 new food industry1

    荒勝俊( Part： Edit, 東洋医学 薬膳)

    荒勝俊（国会図書館所蔵 23554536）  2011

  • Bacterial DNA, DNA polymerase and DNA helicases

    Knudsen, Walter D., Bruns, Sam S.( Part： Contributor, Genome Reduction in Bacillus subtilis and Enhanced Productivities of Recombinant Proteins)

    Nova Science  2010.04 ISBN: 160741094X

    ASIN

  • 技術コンサルティングハンドブック

    日本技術士会プロジェクトチーム技術図書刊行会( Part： Contributor, 安全管理)

    オーム社  2009.01 ISBN: 9784274206535

  • 微生物機能を活用した革新的生産技術の最前線 : ミニマムゲノムファクトリーとシステムバイオロジー

    清水, 昌, 大竹, 久夫, 藤尾, 達郎, 穴澤, 秀治(枯草菌のミニマムゲノムファクトリー)

    シーエムシー出版  2007.12 ISBN: 9784882319702

  • 技術士ハンドブック

    日本技術士会プロジェクトチーム技術図書刊行会( Part： Contributor, 科学者の倫理)

    オーム社  2006.11 ISBN: 4274203069

    ASIN

  • Software state-of-the-art : selected paper

    ( Part： Joint translator, Communications of ACM)

    2006.09 ISBN: 4798110612

  • バイオテクノロジー総覧

    日本能率協会総合研究所( Part： Contributor, バイオに関する倫理、個人情報保護)

    通産資料出版会  2005.04 ISBN: 490186405X

    ASIN

  • 先端技術の個人情報保護 : 生命科学・情報科学・技術倫理の考え方

    奥田, 孝之, 荒, 勝俊, 山野, 浩

    地人書館  2003.01 ISBN: 4805207221

▼display all

Presentations

  • 枯草菌の胞子形成細胞におけるﾘﾎﾞｿｰﾑの二量体化

    前橋真利江, 加増祐佳, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    The 82nd Annual Meeting of GSJ 

    Presentation date： 2010

  • 枯草菌定常期におけるﾀﾞｲﾏｰﾘﾎﾞｿｰﾑ及びyvyD遺伝子の機能解析

    加増祐佳, 前橋真利江, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    The 82nd Annual Meeting of GSJ 

    Presentation date： 2010

  • 枯草菌におけるｽﾄﾚｽ処理によるﾀﾞｲﾏｰﾘﾎﾞｿｰﾑ形成誘導

    星野将太, 和田哲也, 鈴木祥太, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    The 82nd Annual Meeting of GSJ 

    Presentation date： 2010

  • 枯草菌を宿主とした菌体外分泌によるﾋﾄ型異種ﾀﾝﾊﾟｸ質生産 -AmyE プロ配列の付加は、hIFN-2bの分泌を促進する-

    掛下大視, 影山泰, 荒勝俊, 尾崎克也, 中村幸治

    2010年ｸﾞﾗﾑ陽性菌研究会 

    Presentation date： 2010

  • 枯草菌細胞壁のｱﾆｵﾝ性ﾎﾟﾘﾏｰ組成改変株に関して

    児玉武子, 両角俊明, 荒勝俊, 尾崎克也, 関口順一

    2010年ｸﾞﾗﾑ陽性菌研究会 

    Presentation date： 2010

  • 枯草菌ｹﾞﾉﾑ縮小株による蛋白質高生産

    影山泰, 森本拓也, 眞鍋憲二, 劉生浩, 小澤忠弘, 遠藤圭二, 澤田和久, 東畑正敏, 掛下大視, 児玉武子, 荒勝俊, 尾崎克也, 金谷重彦, 田中暉夫, 藤田泰太郎, 河村富士夫, 中村幸治, 山根國男, 橋本昌征, 関口順一, 小笠原直毅

    2010年ｸﾞﾗﾑ陽性菌研究会 

    Presentation date： 2010

  • 枯草菌ｹﾞﾉﾑ工学によるｾﾙﾗｰｾﾞ高発現宿主の開発

    劉生浩, 遠藤圭二, 澤田和久, 東畑正敏, 小澤忠弘, 影山泰, 眞鍋憲二, 荒勝俊, 尾崎克也

    平成22年度ｾﾙﾗｰｾﾞ研究会 

    Presentation date： 2010

  • 枯草菌新奇ppGpp合成酵素YwaCによるﾘﾎﾞｿｰﾑの二量体化機構の解析

    田上和美, 増田健太, 前橋真利恵, 吉田昌樹, 黒岩晴子, 黒岩常祥, 七宮英晃, 劉生浩, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    平成22年度日本農芸化学会 

    Presentation date： 2010

  • 枯草菌を宿主とした菌体外分泌によるﾀﾝﾊﾟｸ質生産

    掛下大視, 影山泰, 荒勝俊, 尾崎克也, 中村幸治

    平成22年度日本農芸化学会ｼﾝﾎﾟｼﾞｭｰﾑ 

    Presentation date： 2010

  • Effect of rocG expression on recombinant enzyme productivity in a Bacillus subtilis strain with a reduced genome

    K. Manabe, Y. Kageyama, T. Ozawa, E. Shimizu, T. Morimoto, K. Ara, K. Ozaki, S. Kanaya, N. Ogasawara

    11th International Symposium on the Genetics of Industrial Microorganisms 

    Presentation date： 2010

  • Properties of a Bacillus subtilis strain with a reduced genome

    Y. Kageyama, R.Kadoya, K. Endo, M. Tohata, K. Sawada, S. Liu, T. Ozawa, K. Manabe, K. Ara, K. Ozaki, N. Ogasawara

    11th International Symposium on the Genetics of Industrial Microorganisms 

    Presentation date： 2010

  • 枯草菌における新規ppGpp合成酵素YwaCの生体内機能とﾘﾎﾞｿｰﾑの二量体化機構の解析

    田上和美, 増田健太, 前橋真利江, 廣畑吉崇, 吉田昌樹, 黒岩晴子, 黒岩常祥, 七宮英晃, 戸澤譲, 劉生浩, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    平成21年度日本遺伝学会 

    Presentation date： 2009

  • 枯草菌における新奇ppGpp合成酵素YwaCによるﾀﾞｲﾏｰﾘﾎﾞｿｰﾑ形成の解析

    田上和美, 平岡紘奈, 松井直子, 増田健太, 吉田昌樹, 黒岩晴子, 黒岩常祥, 七宮英晃, 劉生浩, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    平成21年度日本農芸化学会 

    Presentation date： 2009

  • 枯草菌における分子ｼｬﾍﾟﾛﾝを用いた異種ﾀﾝﾊﾟｸ質の分泌生産

    掛下大視, 劉生浩, 荒勝俊, 尾崎克也, 中村幸治

    平成21年度日本農芸化学会 

    Presentation date： 2009

  • 枯草菌ｹﾞﾉﾑ縮小株の酵素生産におけるｸﾞﾙﾀﾐﾝ酸ﾃﾞﾋﾄﾞﾛｹﾞﾅｰｾﾞの役割

    影山泰, 眞鍋憲二, 森本拓也, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    平成21年度日本農芸化学会 

    Presentation date： 2009

  • 枯草菌ｹﾞﾉﾑ縮小株の酵素高生産因子の解明

    眞鍋憲二, 影山泰, 東畑正敏, 遠藤圭二, 森本拓也, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    平成21年度日本農芸化学会 

    Presentation date： 2009

  • 枯草菌yjeAのﾍﾟﾌﾟﾁﾄﾞｸﾞﾘｶﾝ糖鎖のﾃﾞｱｾﾁﾗｰｾﾞ活性に関する解析

    小林香織, 児玉武子, 小林香織, 荒勝俊, 尾崎克也, 福島達也, 関口順一

    平成21年度日本ｹﾞﾉﾑ微生物学会 

    Presentation date： 2009

  • 枯草菌ｹﾞﾉﾑ縮小株のﾄﾗﾝｽｸﾘﾌﾟﾄｰﾑ解析

    森本拓也, 影山泰, 眞鍋憲二, 荒勝俊, 尾崎克也, 小笠原直毅

    平成21年度日本ｹﾞﾉﾑ微生物学会 

    Presentation date： 2009

  • Production of a Bacillus subtilis strain with a reduced genome

    荒勝俊, 影山泰, 尾崎克也, 小笠原直毅

    第82回日本細菌学会国際ｼﾝﾎﾟｼﾞｭｰﾑ 

    Presentation date： 2009

  • Reprogramming of the metabolic network in a Bacillus subtilis strain depleted of 874 kb of the genomic sequence

    T. Morimoto, Y. Kageyama, K. Manabe, K. Ara, K. Ozaki, N. Ogasawara

    The 4th European Conference on Prokaryotic Genomics 

    Presentation date： 2009

  • Enhanced recombinant protein productivity by genome reduction in Bacillus subtilis

    K. Ara, N. Ogasawara

    The 4th European Conference on Prokaryotic Genomics 

    Presentation date： 2009

  • Characterization of gene products regulated by the essential two-component system in Bacillus subtilis

    K. Kobayashi, T. Fukushima, H. Yamamoto, T. Kodama, K. Ara, K. Ozaki, J. Sekiguchi

    Presentation date： 2009

  • PdaC deacetylates the acetyl groups of N-acetylglucosamine in chitin oligomers and N-acetymuramic acid in peptidoglycan -Biochemical approach for identification of YjeA (PdaC) in Bacillus subtilis -

    K. Kobayashi, T. Kodama, T. Fukushima, K. Ara, K. Ozaki, J. Sekiguchi

    Functional genomics of Gram-positive microorganisms 

    Presentation date： 2009

  • 枯草菌ｹﾞﾉﾑ工学によるﾀﾝﾊﾟｸ質高発現宿主の開発

    尾崎克也, 荒勝俊

    平成20年度日本生物工学会ｼﾝﾎﾟｼﾞｭｰﾑ 

    Presentation date： 2008

  • 枯草菌MGF

    荒勝俊

    日本化学会第88回春季年会ATPﾌﾟﾛｸﾞﾗﾑ依頼講演 

    Presentation date： 2008

  • 枯草菌SecAのC末端領域の解析

    掛下大規, 影山泰, 荒勝俊, 尾崎克也, 中村幸治

    平成20年度日本農芸化学会 

    Presentation date： 2008

  • 枯草菌ｹﾞﾉﾑ縮小株のﾄﾗﾝｽｸﾘﾌﾟﾄｰﾑ解析

    森本拓也, 影山泰, 眞鍋憲二, 児玉武子, 荒勝俊, 尾崎克也, 小笠原直毅

    平成20年度日本ｹﾞﾉﾑ微生物学会 

    Presentation date： 2008

  • 枯草菌ｹﾞﾉﾑ縮小株のﾄﾗﾝｽｸﾘﾌﾟﾄｰﾑ解析

    森本拓也, 影山泰, 眞鍋憲二, 児玉武子, 荒勝俊, 尾崎克也, 小笠原直毅

    BMB2007:第30回日本分子生物学会大会 

    Presentation date： 2007

  • 枯草菌のyjeAの多糖ﾃﾞｱｾﾁﾗｰｾﾞ活性に関する解析

    児玉武子, 小林香織, 荒勝俊, 尾崎克也, 関口順一

    平成19年度日本生物工学会 

    Presentation date： 2007

  • 枯草菌によるﾘﾊﾟｰｾﾞLipA発現系の開発

    眞鍋憲二, 影山泰, 児玉武子, 遠藤圭二, 荒勝俊, 関口順一

    平成19年度日本生物工学会 

    Presentation date： 2007

  • 枯草菌AraRﾘﾌﾟﾚｯｻｰとそれに抑制されるaraAﾌﾟﾛﾓｰﾀｰを用いたﾏｰｶｰﾌﾘｰ遺伝子削除法の検討

    劉生浩, 遠藤圭二, 荒勝俊, 尾崎克也

    平成19年度日本農芸化学会 

    Presentation date： 2007

  • 枯草菌ｹﾞﾉﾑ大領域欠失株の解析

    影山泰, 澤田和久, 東畑正敏, 遠藤圭二, 劉生浩, 小澤忠弘, 眞鍋憲二, 荒勝俊, 尾崎克也, 小笠原直毅

    平成19年度日本農芸化学会 

    Presentation date： 2007

  • 枯草菌における非翻訳型RNA，BS101の機能解析

    掛下大規, 荒勝俊, 中村幸治

    平成19年度日本農芸化学会 

    Presentation date： 2007

  • 枯草菌AprXﾌﾟﾛﾃｱｰｾﾞは細胞増殖の定常期後期に異種分泌ﾀﾝﾊﾟｸ質を分解する

    児玉武子, 遠藤圭二, 荒勝俊, 尾崎克也, 掛下大規, 山根國男, 関口順一

    平成19年度日本ｹﾞﾉﾑ微生物学会 

    Presentation date： 2007

  • ｽﾙﾒｲｶ墨袋からの効率的な墨の回収と精製に関する研究

    川内谷千晶, 上野孝, 荒勝俊, 田谷嘉浩, 下野巧

    第9回化学工学会・学生発表会（東京大会） 

    Presentation date： 2007

  • Enhanced recombinant protein productivity by genome reduction in Bacillus subtilis

    T. Morimoto, K. Ara, K. Ozaki, N. Ogasawara

    The University of Tokyo International Symposium 

    Presentation date： 2007

  • Bacillus subtilis AprX involved in degradation of a heterologoous protein during the late stationary growth phase

    T. Kodama, K. Endo, K. Sawada, K. Ara, K. Ozaki, H. Kakeshita, K. Yamane, J. Sekiguchi

    Functional genomics of Gram-positive microorganisms 

    Presentation date： 2007

  • Prorerties of a Bacillus subtilis strain with a reduced genome

    Y. Kageyama, R. Kadoya, K. Endo, M. Tohata, K. Sawada, S. Liu, T. Ozawa, K. Manabe, K. Ara, K. Ozaki, N. Ogasawara

    Functional genomics of Gram-positive microorganisms 

    Presentation date： 2007

  • Enhanced heterogous production of human interferonα by Bacillus subtilis expressing mutant SecA lacking the extreme C-terminal domain(CTD)

    D. Kakeshita, K. Endo, K. Ara, K. Ozaki, K. Nakamura

    Functional genomics of Gram-positive microorganisms 

    Presentation date： 2007

  • Recent progress in human salivary cystatin research

    E. Saitoh, T. Kato, K. Minaguch, K. Okuda, Y. Hayashi, S. Akiba, K. Ara

    10th Symposium on proteinase inhibitors and biological control 

    Presentation date： 2007

  • 動脈産業の根幹を支える宿主細胞創始に向けて（枯草菌MGFの開発）

    荒勝俊

    平成18年度日本生物工学会ｼﾝﾎﾟｼﾞｭｰﾑ 

    Presentation date： 2006

  • 枯草菌ＭＧＦの開発研究（2）

    遠藤圭二, 東畑正敏, 劉生浩, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    平成18年度日本農芸化学会 

    Presentation date： 2006

  • 枯草菌ＭＧＦの開発研究（1）

    東畑正敏○、澤田和久、遠藤圭二、劉生浩、小澤忠弘、荒勝俊、尾崎克也, 小笠原直毅

    平成18年度日本農芸化学会 

    Presentation date： 2006

  • 細胞間情報伝達関連遺伝子の欠失による酵素生産性の向上

    澤田和久, 東畑正敏, 遠藤圭二, 劉生浩, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    平成18年度日本農芸化学会 

    Presentation date： 2006

  • OGHﾏｲｸﾛｱﾚｲ法を用いたｱﾐﾗｰｾﾞ高生産性Bacillus subtilis 2633染色体上のamyE-tmrB遺伝子近辺領域の構造編成の解析

    掛下大規, 遠藤圭二, 荒勝俊, 尾崎克也, 中村幸治

    平成18年度日本農芸化学会 

    Presentation date： 2006

  • 枯草菌ｹﾞﾉﾑの縮小

    門屋亨介, 荒勝俊, 尾崎克也, 小笠原直毅

    平成18年度日本農芸化学会 

    Presentation date： 2006

  • 枯草菌ｹﾞﾉﾑの人為的縮小

    門屋亨介, 荒勝俊, 尾崎克也, 小笠原直毅

    文部科学省特定領域ｹﾞﾉﾑ４領域第８回ﾜｰｸｼｮｯﾌﾟ 

    Presentation date： 2006

  • 枯草菌ｹﾞﾉﾑの人為的縮小

    門屋亨介, 荒勝俊, 尾崎克也, 小笠原直毅

    平成17年度日本分子生物学会 

    Presentation date： 2005

  • 単分散ｲｶ墨色素粒子の分離精製濃縮ﾌﾟﾛｾｽの開発

    上野孝○、木村絵梨子、山田拓也、荒勝俊、小林淳哉、田谷嘉浩、下野巧

    平成17年度日本生物工学会 

    Presentation date： 2005

  • 枯草菌Spo0A変異株の溶菌抑制に関する解析

    児玉武子, 遠藤圭二, 荒勝俊, 尾崎克也, 関口順一

    平成17年度日本生物工学会 

    Presentation date： 2005

  • 枯草菌ｹﾞﾉﾑ大領域の一括置換方法の検討

    劉生浩, 遠藤圭二, 澤田和久, 東畑正敏, 荒勝俊, 尾崎克也

    平成17年度日本生物工学会 

    Presentation date： 2005

  • A study on the mass production system of recombinant human saline cystatins

    斉藤英一, 林康弘, 秋葉俊一, 荒勝俊

    第78回日本生化学会大会 

    Presentation date： 2005

  • 精製ｲｶ墨色素粒子の特性評価に関する研究

    山本みや子, 上野孝, 荒勝俊, 小林淳哉, 田谷嘉浩, 下野巧

    第7回化学工学会・学生発表会（東日本地区） 

    Presentation date： 2005

  • 単分散ｲｶ墨色素粒子の分離精製方法の開発

    佐々木由香, 上野孝, 荒勝俊, 小林淳哉, 田谷嘉浩, 下野巧

    第7回化学工学会・学生発表会（東日本地区） 

    Presentation date： 2005

  • 枯草菌ｹﾞﾉﾑの人為的縮小の研究

    門屋亨介, 澤田和久, 荒勝俊, 尾崎克也, 小笠原直毅

    平成17年度日本農芸化学会 

    Presentation date： 2005

  • ｾﾙﾗｰｾﾞ高生産変異株(hprK破壊株)の遺伝子発現変動解析

    遠藤圭二, 東畑正敏, 荒勝俊, 尾崎克也

    平成17年度日本農芸化学会 

    Presentation date： 2005

  • Reduction of the Bacillus subtilis genome

    R. Kadoya, K. Ara, K. Ozaki, N. Ogasawara

    Genomes, Medicine and the Environment 

    Presentation date： 2005

  • New deodrant technolosy based on mechanism of apocrine malodor generation

    A. Fuji, T. Hagura, K. Takeuchi, S. Akiba, K. Ara, K. Kusuoka, Y. Hasegawa, M. Yabuki

    Deodrant technology based on mechanism of apocrine malodor generation 

    Presentation date： 2005

  • Zymography of extracellular protease in Bacillus subtilis

    T. Kodama, K. Endo, K. Ara, K. Ozaki, J. Sekiguchi

    Functional genomics of Gram-positive microorganisms 

    Presentation date： 2005

  • Gene amplification of Bacillus subtilis 2633 genome revealed by comparative genomic hybridization microarray

    D. Kakeshita, K. Nakamura, K. Endo, K. Ara, K. Ozaki, K. Yamane

    Functional genomics of Gram-positive microorganisms 

    Presentation date： 2005

  • Development of host microorganisms with optimized protein production

    K. Endo, M. Tohata, S. Liu, K. Sawada, K. Ara, K. Ozaki, K. Kobayashi, N. Ogasawara

    Functional genomics of Gram-positive microorganisms 

    Presentation date： 2005

  • 枯草菌Minimum Genome Factory(MGF)の開発研究

    荒勝俊, 尾崎克也

    日本生物工学会ｼﾝﾎﾟｼﾞｭｰﾑ 

    Presentation date： 2004

  • 枯草菌ｹﾞﾉﾑ情報を利用した産業用宿主細胞の創製

    澤田和久, 遠藤圭二, 東畑正敏, 劉生浩, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    平成16年度日本生物工学会 

    Presentation date： 2004

  • 枯草菌遺伝子破壊・欠失株ﾗｲﾌﾞﾗﾘｰの酵素生産性評価

    東畑正敏, 遠藤圭二, 澤田和久, 小澤忠弘, 荒勝俊, 尾崎克也, 小林和夫, 小笠原直毅

    平成16年度日本生物工学会 

    Presentation date： 2004

  • ｲｶ墨袋からの単分散ｲｶ墨色素粒子の分離精製

    上野孝, 上山哲郎, 荒勝俊, 田谷嘉浩, 下野巧

    第51回日本食品科学工学会 

    Presentation date： 2004

  • 住宅における真菌の季節変動

    藪根ちあき, 荒勝俊, 小島みゆき, 田中辰明

    日本建築学会 

    Presentation date： 2004

  • 寝室と寝具における真菌の動態

    藪根ちあき, 田中辰明, 荒勝俊, 小島みゆき, 相原真紀, 高鳥浩介

    第31回日本防菌防黴学会 

    Presentation date： 2004

  • 家庭内生活環境（玄関、ﾄｲﾚ）における真菌分布変化

    荒勝俊, 相原真紀, 小島みゆき, 都島康彦, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    第31回日本防菌防黴学会 

    Presentation date： 2004

  • ｲｶ墨からのｲｶ墨色素粒子の分離精製

    上山哲郎, 上野孝, 荒勝俊, 田谷嘉浩, 下野巧

    第6回化学工学会・学生発表会（東日本地区） 

    Presentation date： 2004

  • Efficient production of human salivary cystatins by Bacillus subtilis

    K. Ara, S. Akiba, Y. Hayashi, Y. Hakamada, K. Endo, S. Kawai, E. Saitoh

    154th Meeting Society for general Microbiology 

    Presentation date： 2004

  • 家庭内生活環境（押入れ、ｸﾛｰｾﾞｯﾄ）における真菌分布変化

    荒勝俊, 相原真紀, 小島みゆき, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    第47回日本医真菌学会 

    Presentation date： 2003

  • 寝具・床などのﾀﾞﾆ・真菌・細菌の生息実態と相互関係

    上田伸男, 陳鋼, 荒勝俊, 高岡正敏

    第34回日本職業・環境ｱﾚﾙｷﾞｰ学会 

    Presentation date： 2003

  • 家庭における生活者のｶﾋﾞ意識と真菌分布

    小島みゆき, 都島康彦, 小屋たえ子, 荒勝俊, 上田伸男, 秋山一男, 高鳥浩介

    第30回日本防菌防黴学会 

    Presentation date： 2003

  • 家庭内生活環境（寝室、寝具）における真菌分布変化

    荒勝俊, 相原真紀, 小島みゆき, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    第30回日本防菌防黴学会 

    Presentation date： 2003

  • 細菌分布および生活意識・行動からみた家庭の衛生対策

    小島みゆき, 都島康彦, 小屋たえ子, 荒勝俊

    日本油化学会 

    Presentation date： 2002

  • 家庭内生活環境（ﾘﾋﾞﾝｸﾞ、和室）における真菌分布変化

    荒勝俊, 相原真紀, 小島みゆき, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    第46回日本医真菌学会 

    Presentation date： 2002

  • 屋内生活環境－浴室・洗面所－の真菌分布

    相原真紀, 荒勝俊, 小島みゆき, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    第29回日本防菌防黴学会 

    Presentation date： 2002

  • ｽﾀﾝﾌﾟ法を用いた白癬菌の分離－安全靴の検討－

    入交純也, 加藤卓朗, 谷口祐子, 西岡清, 荒勝俊

    第101回日本皮膚科学会総会 

    Presentation date： 2002

  • 住居内のカビの動態調査（ｷｯﾁﾝの真菌分布変化）

    荒勝俊, 相原真紀, 小島みゆき, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    日本ｱﾚﾙｷﾞｰ学会 

    Presentation date： 2002

  • 皮膚の常在菌を殺さずにﾆｵｲを抑える新機構の防臭剤

    荒勝俊

    HOBIA（特別講演会） 

    Presentation date： 2002

  • 家庭内住環境における真菌の動態および分布ﾏｯﾌﾟ作成

    高鳥浩介, 荒勝俊, 徳田一, 川合修次, 上田伸男, 秋山一男

    第45回日本医真菌学会 

    Presentation date： 2001

  • 有胞子乳酸菌と健康

    荒勝俊, 川合修次

    日本生物工学会総会（ｼﾝﾎﾟｼﾞｭｰﾑ） 

    Presentation date： 2001

  • 家庭における細菌分布と生活者の意識・行動に関する調査報告

    小島みゆき, 都島康彦, 小屋たえ子, 荒勝俊, 川合修次

    日本防菌防黴学会 

    Presentation date： 2001

  • 長期ﾍﾞｯﾄﾞﾚｽﾄﾍｯﾄﾞﾀﾞｳﾝ法による腸内細菌属の変化

    上田伸男, 荒勝俊, 渡邊高明, 陳鋼, 福岡秀興

    第2回ﾍﾞｯﾄﾞﾚｽﾄ研究報告会 

    Presentation date： 2001

  • 乳酸菌の健康

    荒勝俊, 川合修次

    日本生物工学会乳酸菌工学部会 

    Presentation date： 2001

  • 足白癬の実態調査 第３報 ﾌﾞｰﾂ着用女性

    加藤卓朗, 渡部京子, 谷口祐子, 西岡清, 沖坂浩一, 荒勝俊

    第100回日本皮膚科学会総会 

    Presentation date： 2001

  • 会社施設における被験者の足底への白癬菌の付着状況－社員寮とﾛｯｶｰ室の検討－

    谷口祐子, 西岡清, 加藤卓朗, 浜正勝, 荒勝俊

    第100回日本皮膚科学会総会 

    Presentation date： 2001

  • 足白癬の実態調査 その２ 会社員（研究職）

    渡部京子, 谷口祐子, 西岡清, 加藤卓朗, 荒勝俊, 茅根滋人

    第44回日本医真菌学会 

    Presentation date： 2000

  • 会社社員寮における被験者の足底への白癬菌の付着状況

    谷口祐子, 西岡清, 加藤卓朗, 荒勝俊, 森啓

    第44回日本医真菌学会 

    Presentation date： 2000

  • Alkaline enzymes from alkaliphiles

    S.Ito○, T.Kobayashi, K.Ara, S.Kawai, K.Ozaki, Y.Hatada

    International Congress on Extremophiles 

    Presentation date： 1998

  • Alkaline amylolytic enzymes produced by strains of alkalophilic Bacillus

    K. Igarashi, K. Ara, H. Hagihara, Y. Hatada, T. Kobayashi, S. Kawai, S. Ito

    37th International detergency conference 

    Presentation date： 1996

  • 好ｱﾙｶﾘ性菌と有用酵素

    伊藤進, 川合修次, 小林徹, 荒勝俊, 尾崎克也

    平成7年度日本生物工学大会ｼﾝﾎﾟｼﾞｭｰﾑ 

    Presentation date： 1995

  • 好ｱﾙｶﾘ性Bacillus sp. KSM-AP1378の生産するｱﾙｶﾘｱﾐﾛﾌﾟﾙﾗﾅｰｾﾞ遺伝子の解析

    秦田勇二, 五十嵐一暁, 荒勝俊, 尾崎克也, 川合修次, 伊藤進

    1995年度日本農芸化学会大会 

    Presentation date： 1995

  • 好ｱﾙｶﾘ性Bacillus sp. KSM-AP1378の生産するｱﾙｶﾘ液化型α-ｱﾐﾗｰｾﾞ遺伝子の解析

    五十嵐一暁, 秦田勇二, 尾崎克也, 荒勝俊, 小林徹, 川合修次, 伊藤進

    1995年度日本農芸化学会大会 

    Presentation date： 1995

  • 好ｱﾙｶﾘ性Bacillus sp. KSM-AP1378の生産する洗剤用ｱﾙｶﾘ液化型αｱﾐﾗｰｾﾞの性質

    荒勝俊, 萩原浩, 五十嵐一暁, 澤田和久, 佐伯勝久, 小林徹, 伊藤進

    1995年度日本農芸化学会大会 

    Presentation date： 1995

  • 好ｱﾙｶﾘ性Bacillus sp. KSM-AP1378の生産する洗剤用ｱﾙｶﾘﾌﾟﾙﾗﾅｰｾﾞの性質

    荒勝俊, 萩原浩, 五十嵐一暁, 澤田和久, 佐伯勝久, 高岩美喜雄, 川合修次, 伊藤進

    1995年度日本農芸化学会大会 

    Presentation date： 1995

  • 好ｱﾙｶﾘﾌﾟﾙﾗﾅｰｾをﾞｺｰﾄﾞする遺伝子解析

    五十嵐一暁, 荒勝俊, 佐伯勝久, 伊藤進

    1993年度日本農芸化学会大会 

    Presentation date： 1993

  • 好ｱﾙｶﾘ性Bacillus属細菌の生産するｱﾙｶﾘｲｿｱﾐﾗｰｾﾞの精製及び諸性質の検討

    荒勝俊, 佐伯勝久, 五十嵐一暁, 伊藤進

    1993年度日本農芸化学会大会 

    Presentation date： 1993

  • 好ｱﾙｶﾘ性Bacillus属細菌の生産するｱﾙｶﾘﾌﾟﾙﾗﾅｰｾﾞの精製及び諸性質の検討

    荒勝俊, 五十嵐一暁, 佐伯勝久, 伊藤進

    1993年度日本農芸化学会大会 

    Presentation date： 1993

  • ﾛﾄﾞｺｯｶｽ属菌によるｱﾙｷﾙ化合物の不飽和化反応

    小池謙造, 高岩美喜雄, 荒勝俊, 足立重仁, 滝川博文, 伊藤進

    1989年度日本醗酵工学会大会 

    Presentation date： 1989

  • 中性Bacillus属細菌の生産するｱﾙｶﾘｾﾙﾗｰｾﾞの精製及び諸性質の検討

    川合修次, 大越浩美, 押野一志, 荒勝俊, 伊藤進

    1987年度日本農芸化学会大会 

    Presentation date： 1987

  • LASの流水条件下における魚類に及ぼす影響

    荒勝俊, 池田祐三, 吉村孝一

    1983年度水産学会秋季大会 

    Presentation date： 1983

  • 河川水中における界面活性剤の生分解性

    吉村孝一, 荒勝俊, 川瀬次郎, 林克也

    第４７回陸水学会秋季大会 

    Presentation date： 1982

  • Nocardia erythropolisの生産するﾌﾟﾛﾄｶﾃｷﾝ酸酸素添加酵素の精製及び諸性質の検討

    荒勝俊, 倉根隆一郎, 中村以正, 鈴木智雄, 福岡誠一

    1981年度日本発酵工学会秋季大会 

    Presentation date： 1981

▼display all

Misc

  • 早稲田地球再生塾が目指す“Society 5.0+”の世界

    荒勝俊, 木野邦器

    生物工学会誌   96 ( 12 ) 720 - 721  2018.12

    Authorship：Lead author

    Article, review, commentary, editorial, etc. (scientific journal)  

  • SDGs目標達成に向けた 科学技術イノベーションの貢献 「早稲田地球再生塾（WERS）が果たす役割」

    荒勝俊, 木野邦器

    バイオサイエンスとインダストリー   76 ( 4 ) 334 - 337  2018.04

    Authorship：Lead author

  • 藻類バイオ燃料の開発最前線

    荒勝俊

    エネルギー・資源   37 ( 4 )  2016

    J-GLOBAL

  • “薬膳”の知恵(83)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   56 ( 3 )  2014

    J-GLOBAL

  • “薬膳”の知恵(82)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   56 ( 2 )  2014

    J-GLOBAL

  • Creation of novel technologies for extracellular protein production toward the development of bacillus subtilis genome factories

    Katsutoshi Ara, Kenji Manabe, Shenghao Liu, Yasushi Kageyama, Tadahiro Ozawa, Masatoshi Tohata, Keiji Endo, Kazuhisa Sawada, Nozomu Shibata, Akihito Kawahara, Kazuhiro Saito, Hiroshi Kodama, Yoshiharu Kimura, Katsuya Ozaki, Yoshinori Takema, Hiroshi Kakeshita, Kouji Nakamura, Kunio Yamane, Takeko Kodama, Junichi Sekiguchi, Takuya Morimoto, Ryosuke Kadoya, Shigehiko Kanaya, Yasutaro Fujita, Fujio Kawamura, Naotake Ogasawara

    Microbial Production: From Genome Design to Cell Engineering     3 - 15  2013.11

    　View Summary

    Bacillus subtilis has been widely used for the industrial production of useful proteins because of its high protein secretion ability and safety. We focused on genome reduction as a new concept for enhancing production of recombinant enzymes in B. subtilis cells based on detailed analysis of the genome mechanism. First, we reported that a novel B. subtilis strain, MGB874, depleted 20.7 % of the genomic sequence of the wild type by rationally designed deletions to create simplified cells for protein production. When compared with wild-type cells, the productivity of cellulase and protease from transformed plasmids harboring the corresponding genes was markedly enhanced. These results indicate that a bacterial factory specializing in the production of substances can be constructed by deleting the genomic regions unimportant for growth and substance production from B. subtilis. Second, deletion of the rocDEF-rocR region, which is involved in arginine degradation, was found to contribute to the improvement of enzyme production in strain MGB874. The present study indicated that our results demonstrated the effectiveness of a synthetic genomic approach with reduction of genome size to generate novel and useful bacteria for industrial uses. Furthermore, the design of the changes in the transcriptional regulatory network of the nitrogen metabolic pathway in B. subtilis cells could facilitate the generation of improved industrial protein production.

    DOI

  • “薬膳”の知恵(75)

    荒勝俊, 荒勝俊

    New Food Industry   55 ( 4 )  2013

    J-GLOBAL

  • “薬膳”の知恵(76)

    荒勝俊, 荒勝俊

    New Food Industry   55 ( 5 )  2013

    J-GLOBAL

  • “薬膳”の知恵(77)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   55 ( 7 )  2013

    J-GLOBAL

  • “薬膳”の知恵(79)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   55 ( 10 )  2013

    J-GLOBAL

  • “薬膳”の知恵(73)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   55 ( 2 )  2013

    J-GLOBAL

  • “薬膳”の知恵(80)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   55 ( 11 )  2013

    J-GLOBAL

  • “薬膳”の知恵(78)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   55 ( 9 )  2013

    J-GLOBAL

  • “薬膳”の知恵(81)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   55 ( 12 )  2013

    J-GLOBAL

  • “薬膳”の知恵(74)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   55 ( 3 )  2013

    J-GLOBAL

  • “薬膳”の知恵(69)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   54 ( 8 )  2012

    J-GLOBAL

  • “薬膳”の知恵(67)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   54 ( 6 )  2012

    J-GLOBAL

  • “薬膳”の知恵(65)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   54 ( 4 )  2012

    J-GLOBAL

  • “薬膳”の知恵(71)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   54 ( 11 )  2012

    J-GLOBAL

  • “薬膳”の知恵(70)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   54 ( 9 )  2012

    J-GLOBAL

  • “薬膳”の知恵(72)

    荒勝俊, 荒勝俊

    New Food Industry   54 ( 12 )  2012

    J-GLOBAL

  • “薬膳”の知恵(64)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   54 ( 3 )  2012

    J-GLOBAL

  • “薬膳”の知恵(66)

    荒勝俊, 荒勝俊

    New Food Industry   54 ( 5 )  2012

    J-GLOBAL

  • “薬膳”の知恵(63)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   54 ( 2 )  2012

    J-GLOBAL

  • “薬膳”の知恵(68)

    荒勝俊, 荒勝俊

    New Food Industry   54 ( 7 )  2012

    J-GLOBAL

  • “薬膳”の知恵(62)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   53 ( 11 )  2011

    J-GLOBAL

  • 枯草菌ゲノム大領域欠失株の構築と解析

    影山泰, 森本拓也, 森本拓也, 眞鍋憲二, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    日本農芸化学会大会講演要旨集   2011  2011

    J-GLOBAL

  • “薬膳”の知衷(59)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   53 ( 8 )  2011

    J-GLOBAL

  • ”薬膳”の知恵(57)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   53 ( 6 )  2011

    J-GLOBAL

  • “薬膳”の知恵(54)

    荒勝俊, 荒勝俊

    New Food Industry   53 ( 2 )  2011

    J-GLOBAL

  • “薬膳”の知恵(60)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   53 ( 9 )  2011

    J-GLOBAL

  • “薬膳”の知恵(55)

    荒勝俊, 荒勝俊

    New Food Industry   53 ( 3 )  2011

    J-GLOBAL

  • “薬膳”の知恵(56)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   53 ( 4 )  2011

    J-GLOBAL

  • “薬膳”の知恵(61)

    荒勝俊, 荒勝俊, 荒勝俊

    New Food Industry   53 ( 10 )  2011

    J-GLOBAL

  • “薬膳”の知恵(58)

    荒勝俊, 荒勝俊

    New Food Industry   53 ( 7 )  2011

    J-GLOBAL

  • 枯草菌胞子形成時に発現する新規低分子RNAの同定と機能解析

    山本達也, 掛下大視, 掛下大視, 児玉武子, 森本拓也, 荒勝俊, 尾崎克也, 中村幸治

    日本農芸化学会大会講演要旨集   2011  2011

    J-GLOBAL

  • 枯草菌を宿主としたヒト型インターフェロンα生産時のトランスクリプトーム解析

    掛下大視, 掛下大視, 影山泰, 荒勝俊, 尾崎克也, 中村幸治

    日本農芸化学会大会講演要旨集   2011  2011

    J-GLOBAL

  • ランダム変異を用いた枯草菌Ffhの温度感受性株取得と機能解析

    杉原怜納, 掛下大視, 掛下大視, 影山泰, 荒勝俊, 尾崎克也, 中村幸治

    日本農芸化学会大会講演要旨集   2011  2011

    J-GLOBAL

  • 技術者の倫理と科学者の倫理

    荒勝俊

    月刊技術誌   22 ( 4 ) 4 - 7  2010.04  [Invited]

    Authorship：Lead author

    Article, review, commentary, editorial, etc. (scientific journal)  

  • “薬膳”の知恵(43)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 2 )  2010

    J-GLOBAL

  • ”薬膳”の知恵(44)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 3 )  2010

    J-GLOBAL

  • 技術者の倫理と科学者の倫理

    荒勝俊

    技術士   ( 518 )  2010

    J-GLOBAL

  • 枯草菌新奇ppGpp合成酵素YwaCによるリボソームの二量体化機構の解析

    田上和美, 増田健太, 前橋真利江, 吉田昌樹, 黒岩晴子, 黒岩常祥, 七宮英晃, 劉生浩, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    日本農芸化学会大会講演要旨集   2010  2010

    J-GLOBAL

  • 枯草菌におけるストレス処理によるダイマーリボソーム形成誘導

    星屋将太, 和田哲也, 鈴木祥太, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    日本遺伝学会大会プログラム・予稿集   82nd  2010

    J-GLOBAL

  • 枯草菌定常期におけるダイマーリボソーム及びyvyD遺伝子の機能解析

    加増祐佳, 前橋真利江, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    日本遺伝学会大会プログラム・予稿集   82nd  2010

    J-GLOBAL

  • “薬膳”の知恵(51)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 10 )  2010

    J-GLOBAL

  • “薬膳”の知恵(47)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 6 )  2010

    J-GLOBAL

  • “薬膳”の知恵(45)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 4 )  2010

    J-GLOBAL

  • “薬膳”の知恵(46)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 5 )  2010

    J-GLOBAL

  • “薬膳”の知恵(52)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 11 )  2010

    J-GLOBAL

  • “薬膳”の知恵(49)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 8 )  2010

    J-GLOBAL

  • ”薬膳”の知恵(50)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 9 )  2010

    J-GLOBAL

  • “薬膳”の知恵(53)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 12 )  2010

    J-GLOBAL

  • “薬膳”の知恵(48)

    荒勝俊, 荒勝俊

    New Food Industry   52 ( 7 )  2010

    J-GLOBAL

  • 枯草菌の胞子形成細胞におけるリボソームの二量体化

    前橋真利江, 加増祐佳, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    日本遺伝学会大会プログラム・予稿集   82nd  2010

    J-GLOBAL

  • 枯草菌を宿主とした菌体外分泌によるタンパク質生産

    掛下大視, 掛下大視, 影山泰, 荒勝俊, 尾崎克也, 中村幸治

    日本農芸化学会大会講演要旨集   2010  2010

    J-GLOBAL

  • “薬膳”の知恵(32)

    荒勝俊

    New Food Industry   51 ( 2 )  2009

    J-GLOBAL

  • 枯草菌ゲノム縮小株の酵素生産におけるグルタミン酸デヒドロゲナーゼの役割

    影山泰, 眞鍋憲二, 森本拓也, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    日本農芸化学会大会講演要旨集   2009  2009

    J-GLOBAL

  • 枯草菌ゲノム縮小株の酵素高生産因子の解明

    眞鍋憲二, 影山泰, 東畑正敏, 遠藤圭二, 森本拓也, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    日本農芸化学会大会講演要旨集   2009  2009

    J-GLOBAL

  • “薬膳”の知恵(34)

    荒勝俊

    New Food Industry   51 ( 4 )  2009

    J-GLOBAL

  • “薬膳”の知恵(36)

    荒勝俊

    New Food Industry   51 ( 6 )  2009

    J-GLOBAL

  • “薬膳”の知恵(37)

    荒勝俊, 荒勝俊

    New Food Industry   51 ( 7 )  2009

    J-GLOBAL

  • “薬膳”の知恵(38)

    荒勝俊

    New Food Industry   51 ( 8 )  2009

    J-GLOBAL

  • “薬膳”の知恵(39)

    荒勝俊, 荒勝俊

    New Food Industry   51 ( 9 )  2009

    J-GLOBAL

  • “薬膳”の知恵(41)

    荒勝俊, 荒勝俊

    New Food Industry   51 ( 11 )  2009

    J-GLOBAL

  • “薬膳”の知恵(42)

    荒勝俊, 荒勝俊

    New Food Industry   51 ( 12 )  2009

    J-GLOBAL

  • “薬膳”の知恵(33)

    荒勝俊

    New Food Industry   51 ( 3 )  2009

    J-GLOBAL

  • “薬膳”の知恵(40)

    荒勝俊, 荒勝俊

    New Food Industry   51 ( 10 )  2009

    J-GLOBAL

  • “薬膳”の知恵(35)

    荒勝俊

    New Food Industry   51 ( 5 )  2009

    J-GLOBAL

  • 枯草菌ゲノム工学によるタンパク質高発現宿主の開発

    尾崎克也, 荒勝俊

    発酵と代謝研究会シンポジウム講演要旨集   2009  2009

    J-GLOBAL

  • 枯草菌における新奇ppGpp合成酵素YwaCにおけるダイマーリボソーム形成の解析

    田上和美, 平岡紘奈, 松井直子, 増田健太, 吉田昌樹, 黒岩晴子, 黒岩常祥, 七宮英晃, 劉生浩, 影山泰, 荒克俊, 尾崎克也, 河村富士夫

    日本農芸化学会大会講演要旨集   2009  2009

    J-GLOBAL

  • 枯草菌における分子シャペロンを用いた異種タンパク質の分泌生産

    掛下大視, 掛下大視, 劉生浩, 荒勝俊, 尾崎克也, 中村幸治

    日本農芸化学会大会講演要旨集   2009  2009

    J-GLOBAL

  • 枯草菌における新奇ppGpp合成酵素YwaCの生体内機能とリボソームの二量体化機構の解析

    田上和美, 増田健太, 前橋真利江, 廣畑吉崇, 吉田昌樹, 黒岩晴子, 黒岩常祥, 七宮英晃, 戸澤譲, 劉生浩, 影山泰, 荒勝俊, 尾崎克也, 河村富士夫

    日本遺伝学会大会プログラム・予稿集   81st  2009

    J-GLOBAL

  • ものづくり研究の醍醐味

    荒勝俊

    生物工学会誌   86 ( 5 ) 246 - 247  2008.05  [Invited]

    Authorship：Lead author

    Article, review, commentary, editorial, etc. (scientific journal)  

  • JBAｸﾞﾘｰﾝﾊﾞｲｵ戦略ﾌｫｰﾗﾑ ﾊﾞｲｵﾏｽ分科会報告書

    倉根隆一郎, 鮫島正浩, 五十嵐泰夫, 近藤昭彦, 森川康, 植田充美, 中村暢文, 太田大策, 渡邊隆司, 封馬誠也, 北本宏子, 斉木隆, 磯貝宰, 中川隆, 浜祐子, 東田英毅, 横暮豊一, 小山修, 上野嘉之, 守屋彰悟, 重松義也, 向山正治, 梅田到, 中川正, 中村圭寛, 松本圭司, 穴澤秀治, 西江晴男, 荒勝俊, 泉可也, 田中徹, 種田大介, 荒田芙美子, 矢追克郎, 福永陽子, 矢吹聡一, 塚本芳昭, 地崎修, 伊藤芳弘, 江口有, 福田和彦, 浦尾秀雄, 矢田美恵子, 鈴木奈央

       2008.03

    Internal/External technical report, pre-print, etc.  

  • 平成JBA19年度成果報告書 網羅的解析技術の適用による微生物利用産業の拡大に向けた課題調査

    小笠原直毅, 奥田徹, 加藤秀之, 新井好央, 永井浩二, 新家一男, 伊藤喜久治, 横田篤, 佐々木隆, 鶴岡伸男, 服部憲晃, 矢嶋信浩, 岡村和夫, 渡邊一哉, 高畑陽, 岡崎孝映, 原山重明, 井上恵雄, 穴澤秀治, 荒勝俊, 長澤透, 臼田佳弘, 浜祐子, 松山彰収, 服部正平, 北川正成, 藤田信之, 梶江慎一, 太田大策, 金谷重彦, 小田吉哉, 地崎修, 浦尾秀雄, 矢田美恵子, 鈴木賢一

       2008.03

    Internal/External technical report, pre-print, etc.  

  • “薬膳”の知恵(25)

    荒勝俊

    New Food Industry   50 ( 6 )  2008

    J-GLOBAL

  • “薬膳”の知恵(20)

    荒勝俊

    New Food Industry   50 ( 1 )  2008

    J-GLOBAL

  • “薬膳”の知恵(26)

    荒勝俊

    New Food Industry   50 ( 7 )  2008

    J-GLOBAL

  • “薬膳”の知恵(22)

    荒勝俊

    New Food Industry   50 ( 3 )  2008

    J-GLOBAL

  • “薬膳”の知恵(27)

    荒勝俊

    New Food Industry   50 ( 8 )  2008

    J-GLOBAL

  • 枯草菌ゲノム工学によるタンパク質高発現宿主の開発

    尾崎克也, 荒勝俊

    日本生物工学会大会講演要旨集   60th  2008

    J-GLOBAL

  • 未来を拓くRefined Genome Factory

    荒勝俊

    日本化学会講演予稿集   88th ( 2 )  2008

    J-GLOBAL

  • Characteristics of eumelanin from squids and its utilization

    上野孝, 荒勝俊, 田谷嘉浩, 下野功, 小林孝紀

    日本水産学会誌   74 ( 2 )  2008

    J-GLOBAL

  • “薬膳”の知恵(23)

    荒勝俊

    New Food Industry   50 ( 4 )  2008

    J-GLOBAL

  • “薬膳”の知恵(24)

    荒勝俊

    New Food Industry   50 ( 5 )  2008

    J-GLOBAL

  • “薬膳”の知恵(30)

    荒勝俊

    New Food Industry   50 ( 11 )  2008

    J-GLOBAL

  • “薬膳”の知恵(29)

    荒勝俊

    New Food Industry   50 ( 10 )  2008

    J-GLOBAL

  • “薬膳”の知恵(31)

    荒勝俊

    New Food Industry   50 ( 12 )  2008

    J-GLOBAL

  • “薬膳”の知恵(28)

    荒勝俊

    New Food Industry   50 ( 9 )  2008

    J-GLOBAL

  • “薬膳”の知恵(21)

    荒勝俊

    New Food Industry   50 ( 2 )  2008

    J-GLOBAL

  • 枯草菌SecAのC末端領域の解析

    掛下大規, 掛下大規, 影山泰, 荒勝俊, 尾崎克也, 中村幸治

    日本農芸化学会大会講演要旨集   2008  2008

    J-GLOBAL

  • JBA平成18年度 製品評価技術基盤機構（NITE）委託 微生物資源の分離・濃縮・培養・解析に関する調査 調査報告書

    鎌形洋一, 志津里芳一, 正木春彦, 木野邦器, 岡崎孝映, 富木毅, 金谷重彦, 太田大策, 原山重明, 永井浩二, 大橋武久, 穴澤秀一, 加藤秀之, 荒勝俊, 吉田義則

       2007.03

    Internal/External technical report, pre-print, etc.  

  • “薬膳”の知恵(15)

    荒勝俊

    New Food Industry   49 ( 8 )  2007

    J-GLOBAL

  • 枯草菌における非翻訳型RNA,BS101 RNAの機能解析

    掛下大視, 掛下大視, 五十嵐悠, 荒勝俊, 中村幸治

    日本農芸化学会大会講演要旨集   2007  2007

    J-GLOBAL

  • “薬膳”の知恵(18)

    荒勝俊

    New Food Industry   49 ( 11 )  2007

    J-GLOBAL

  • 枯草菌ゲノム大領域欠失株の解析

    影山泰, 門屋亨介, 遠藤圭二, 東畑正敏, 澤田和久, 劉生浩, 小澤忠弘, 眞鍋憲二, 荒勝俊, 尾崎克也, 小笠原直毅

    日本農芸化学会大会講演要旨集   2007  2007

    J-GLOBAL

  • 枯草菌ゲノム縮小株のトランスクリプトーム解析

    森本拓也, 森本拓也, 影山泰, 眞鍋憲二, 児玉武子, 児玉武子, 荒勝俊, 尾崎克也, 小笠原直毅

    生化学    2007

    J-GLOBAL

  • “薬膳”の知恵(17)

    荒勝俊

    New Food Industry   49 ( 10 )  2007

    J-GLOBAL

  • “薬膳”の知恵(19)

    荒勝俊

    New Food Industry   49 ( 12 )  2007

    J-GLOBAL

  • “薬膳”の知恵(12)

    荒勝俊

    New Food Industry   49 ( 5 )  2007

    J-GLOBAL

  • 枯草菌によるリパーゼLipA発現系の開発

    眞鍋憲二, 影山泰, 児玉武子, 遠藤圭二, 荒勝俊, 関口順一

    日本生物工学会大会講演要旨集   59th  2007

    J-GLOBAL

  • “薬膳”の知恵(13)

    荒勝俊

    New Food Industry   49 ( 6 )  2007

    J-GLOBAL

  • “薬膳”の知恵(16)

    荒勝俊

    New Food Industry   49 ( 9 )  2007

    J-GLOBAL

  • “薬膳”の知恵(8)

    荒勝俊

    New Food Industry   49 ( 1 )  2007

    J-GLOBAL

  • “薬膳”の知恵(14)

    荒勝俊

    New Food Industry   49 ( 7 )  2007

    J-GLOBAL

  • II-2-3.イカ墨ユーメラニン色素の特性とその活用

    上野孝, 荒勝俊, 田谷嘉浩, 下野功, 小林孝紀

    日本水産学会大会講演要旨集   2007  2007

    J-GLOBAL

  • 資源循環型産業・社会構築とバイオインダストリー 動脈産業における高機能性宿主(RGF)の創製研究

    荒勝俊

    生物工学会誌   85 ( 4 )  2007

    J-GLOBAL

  • “薬膳”の知恵(10)

    荒勝俊

    New Food Industry   49 ( 3 )  2007

    J-GLOBAL

  • “薬膳”知恵(11)

    荒勝俊

    New Food Industry   49 ( 4 )  2007

    J-GLOBAL

  • “薬膳”の知恵(9)

    荒勝俊

    New Food Industry   49 ( 2 )  2007

    J-GLOBAL

  • 枯草菌AraRリプレッサーとそれに抑制されるaraAプロモーターを用いたマーカーフリー遺伝子削除法の検討

    劉生浩, 遠藤圭二, 荒勝俊, 尾崎克也

    日本農芸化学会大会講演要旨集   2007  2007

    J-GLOBAL

  • 枯草菌のYjeAの多糖デアセチラーゼ活性に関する解析

    児玉武子, 児玉武子, 小林香織, 荒勝俊, 尾崎克也, 関口順一

    日本生物工学会大会講演要旨集   59th  2007

    J-GLOBAL

  • 東南ｱｼﾞｱにおける乳酸菌資源の学術調査及びﾃﾞｰﾀﾍﾞｰｽの構築（研究課題番号16404020） 平成16年度～17年度科学研究費補助金（基盤研究（B）(１)） 研究成果報告書

    塩谷捨明, 荒勝俊, 岡田早苗, 緒方靖哉, 小原仁実, 片倉啓雄, 門田真理子, 小林元太, 土井梅幸, 土居克実, 酒井謙二, 島純, 園元謙二, 中山二郎, 仁宮一章, 野村善幸, 星野貴行, 山本憲二, 横田篤

       2006.03

    Internal/External technical report, pre-print, etc.  

  • “薬膳”の知恵(1)

    荒勝俊

    New Food Industry   48 ( 6 )  2006

    J-GLOBAL

  • 枯草菌MGF(Minimum Genome Factory)の開発研究-3

    遠藤圭二, 東畑正敏, 澤田和久, 荒勝俊, 尾崎克也, 小林和夫, 小笠原直毅

    日本農芸化学会大会講演要旨集   2006  2006

    J-GLOBAL

  • 枯草菌ゲノムの縮小

    門屋亨介, 門屋亨介, 尾崎克也, 荒勝俊, 小笠原直毅

    日本農芸化学会大会講演要旨集   2006  2006

    J-GLOBAL

  • 枯草菌MGF(Minimum Genome Factory)の開発研究-1

    東畑正敏, 遠藤圭二, 劉生浩, 澤田和久, 小澤忠弘, 荒勝俊, 尾崎克也, 小林和夫, 小笠原直毅

    日本農芸化学会大会講演要旨集   2006  2006

    J-GLOBAL

  • CGHマイクロアレイ法を用いたアミラーゼ高生産株Bucillus subtilis 2633染色体上のamyE-tmrB遺伝子近辺領域の構造編成の解析

    掛下大視, 掛下大視, 遠藤圭二, 荒勝俊, 尾崎克也, 中村幸治

    日本農芸化学会大会講演要旨集   2006  2006

    J-GLOBAL

  • “薬膳”の知恵(5)

    荒勝俊

    New Food Industry   48 ( 10 )  2006

    J-GLOBAL

  • 枯草菌MGF(Minimum Genome Factory)の開発研究-2

    澤田和久, 東畑正敏, 遠藤圭二, 劉生浩, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    日本農芸化学会大会講演要旨集   2006  2006

    J-GLOBAL

  • 動脈産業の根幹を支える宿主細胞創製に向けて(枯草菌MGFの開発)

    荒勝俊

    日本生物工学会大会講演要旨集   58th  2006

    J-GLOBAL

  • “薬膳”の知恵(2)

    荒勝俊

    New Food Industry   48 ( 7 )  2006

    J-GLOBAL

  • “薬膳”の知恵(7)

    荒勝俊

    New Food Industry   48 ( 12 )  2006

    J-GLOBAL

  • “薬膳”の知恵(6)

    荒勝俊

    New Food Industry   48 ( 11 )  2006

    J-GLOBAL

  • “薬膳”の知恵(4)

    荒勝俊

    New Food Industry   48 ( 9 )  2006

    J-GLOBAL

  • 枯草菌ゲノムの人為的縮小

    門屋亨介, 門屋亨介, 荒勝俊, 尾崎克也, 小笠原直毅

    日本分子生物学会年会講演要旨集   28th  2005

    J-GLOBAL

  • 枯草菌ゲノム大領域の一括置換法の検討

    LIU Shenghao, 遠藤圭二, 沢田和久, 東畑正敏, 荒勝俊, 尾崎克也

    日本生物工学会大会講演要旨集   2005  2005

    J-GLOBAL

  • 単分散イカ墨色素粒子の分離精製濃縮プロセスの開発

    上野孝, 木村絵梨子, 山田拓也, 荒勝俊, 田谷嘉浩, 下野功

    日本生物工学会大会講演要旨集   2005  2005

    J-GLOBAL

  • 枯草菌セルラーゼ高生産変異株(hprK遺伝子破壊株)の遺伝子発現変動解析

    遠藤圭二, 東畑正敏, 荒勝俊, 尾崎克也, 小林和夫, 小笠原直毅

    日本農芸化学会大会講演要旨集   2005  2005

    J-GLOBAL

  • 枯草菌ゲノムの人為的縮小の研究

    門屋亨介, 沢田和久, 尾崎克也, 荒勝俊, 小笠原直毅

    日本農芸化学会大会講演要旨集   2005  2005

    J-GLOBAL

  • 発酵食品と健康 6)乳酸菌の保健効果-乳酸菌のゲノム研究(I)-

    荒勝俊

    New Food Industry   47 ( 2 )  2005

    J-GLOBAL

  • 枯草菌spo0A変異株の溶菌抑制に関する解析

    児玉武子, 児玉武子, 遠藤圭二, 荒勝俊, 尾崎克也, 関口順一

    日本生物工学会大会講演要旨集   2005  2005

    J-GLOBAL

  • 発酵食品の健康 7)乳酸菌の保健効果-乳酸菌のゲノム研究(II)-

    荒勝俊

    New Food Industry   47 ( 12 )  2005

    J-GLOBAL

  • イカ墨袋からの単分散イカ墨色素粒子の分離精製

    上野孝, 上山哲郎, 荒勝俊, 田谷嘉浩, 下野巧

    日本食品科学工学会大会講演集   51st  2004

    J-GLOBAL

  • 胞子形成特異的シグマ因子の欠失による酵素生産性の向上

    澤田和久, 遠藤圭二, 東畑正敏, LIU Shenghao, 小澤忠弘, 荒勝俊, 尾崎克也, 小笠原直毅

    日本生物工学会大会講演要旨集   2004  2004

    J-GLOBAL

  • 住宅における真菌の季節変動

    薮根ちあき, 荒勝俊, 小島みゆき, 田中辰明

    日本建築学会学術講演梗概集D-2 環境工学2   2004  2004

    J-GLOBAL

  • 寝室と寝具における真菌の動態

    やぶ根ちあき, 田中辰明, 荒勝俊, 小島みゆき, 相原真紀, 高鳥浩介

    日本防菌防黴学会年次大会要旨集   31st  2004

    J-GLOBAL

  • 家庭内生活環境(玄関・トイレ)における真菌分布変化

    荒勝俊, 相原真紀, 小島みゆき, 都島康彦, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    日本防菌防黴学会年次大会要旨集   31st  2004

    J-GLOBAL

  • Forefront of Science on Lactic Acid Bacteria: Where are we going? The Development of Functional Cosmetics and Food Using Lactic Acid Bacteria

    荒勝俊

    Foods & Food Ingredients Journal of Japan   209 ( 9 )  2004

    J-GLOBAL

  • 枯草菌遺伝子破壊・欠失株ライブラリーの酵素生産性評価

    東畑正敏, 遠藤圭二, 澤田和久, 小澤忠弘, 荒勝俊, 尾崎克也, 小林和夫, 小笠原直毅

    日本生物工学会大会講演要旨集   2004  2004

    J-GLOBAL

  • 発酵食品と健康 5)乳酸菌の保健効果-アレルギー予防効果-

    荒勝俊

    New Food Industry   46 ( 10 )  2004

    J-GLOBAL

  • 枯草菌Minimum Genome Factory(MGF)の開発

    荒勝俊, 尾崎克也

    日本生物工学会大会講演要旨集   2004  2004

    J-GLOBAL

  • Effect of Enzymatic Treatment on Sensory Taste of Soymilk.

    荒勝俊, 吉松正, 小島みゆき, 川合修次, 大久保一良

    日本食品科学工学会誌   50 ( 1 )  2003

    J-GLOBAL

  • 家庭内生活環境(押し入れ,クローゼット)における真菌分布変化

    荒勝俊, 相原真紀, 小島みゆき, 都島康彦, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    日本医真菌学会雑誌   44 ( Supplement 1 )  2003

    J-GLOBAL

  • 酪酸菌の科学

    荒勝俊

    New Food Industry   45 ( 7 )  2003

    J-GLOBAL

  • 家庭内生活環境(寝室・寝具)における真菌分布変化

    荒勝俊, 相原真紀, 小島みゆき, 都島康彦, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    日本防菌防黴学会年次大会要旨集   30th  2003

    J-GLOBAL

  • Effect of Bed Rest on the Intestinal Environment and Microflora in Healthy Young Men

    荒勝俊, 福岡秀興, 石崎優子, 上西一弘, 海老沢秀道, 伊藤昌子, CHEN G, 上田伸男

    栄養学雑誌   61 ( 4 )  2003

    J-GLOBAL

  • 家庭における生活者のカビ意識と真菌分布

    小島みゆき, 都島康彦, 荒勝俊, 相原真紀, 小屋えな子, 上田伸男, 秋山一男, 高鳥浩介

    日本防菌防黴学会年次大会要旨集   30th  2003

    J-GLOBAL

  • プロピオン酸菌の科学

    荒勝俊

    New Food Industry   45 ( 11 )  2003

    J-GLOBAL

  • グルジアの至宝・カスピ海ヨーグルト(グルジアヨーグルト)

    荒勝俊

    New Food Industry   45 ( 3 )  2003

    J-GLOBAL

  • 発酵食品と健康 4) 乳酸菌の保健効果 疾病予防効果

    荒勝俊

    New Food Industry   44 ( 7 )  2002

    J-GLOBAL

  • 屋内生活環境-キッチン-の真菌分布変化

    高鳥浩介, 荒勝俊, 小島みゆき, 都島康彦, 徳田一, 川合修次, 上田伸男, 秋山一男

    アレルギー   51 ( 2/3 )  2002

    J-GLOBAL

  • 発酵食品と健康 乳酸菌の保健効果 3 病原菌感染防御効果

    荒勝俊

    New Food Industry   44 ( 3 )  2002

    J-GLOBAL

  • 屋内生活環境-浴室・洗面所-の真菌分布

    相原真紀, 荒勝俊, 小島みゆき, 都島康彦, 徳田一, 川合修次, 高鳥浩介

    日本防菌防黴学会年次大会要旨集   29th  2002

    J-GLOBAL

  • 乳酸菌工学の未来像 バイオプリザベーションとプロバイオティクス 二つの顔を持つ乳酸菌 有胞子乳酸菌と健康

    荒勝俊, 川合修次

    生物工学会誌   80 ( 12 )  2002

    J-GLOBAL

  • スタンプ法を用いた白せん菌の分離 安全靴の検討

    入交純也, 加藤卓朗, 谷口裕子, 西岡清, 荒勝俊

    日本皮膚科学会雑誌   112 ( 5 )  2002

    J-GLOBAL

  • 家庭内生活環境(リビング,和室)における真菌分布変化

    荒勝俊, 小島みゆき, 相原真紀, 都島康彦, 川合修次, 上田伸男, 秋山一男, 高鳥浩介

    日本医真菌学会雑誌   43 ( Supplement 2 )  2002

    J-GLOBAL

  • Effect of New Lactic Acid Fermentation on Sensory Taste of Fermented Soymilk.

    荒勝俊, 吉松正, 小島みゆき, 川合修次, 大久保一良

    日本食品科学工学会誌   49 ( 6 )  2002

    J-GLOBAL

  • Effects of Locust Bean Gum Intake on Defecation and Intestinal Environment in Healthy Volunteers.

    荒勝俊, 吉松正, 本多泰揮, 川合修次

    腸内細菌学雑誌   15 ( 2 )  2002

    J-GLOBAL

  • Effects on Intestinal Flora of a Beverage Containing Non-fermentable Depolymerized Sodium Alginate and Water-soluble Fermentable Corn Bran Fiber.

    吉松正, 小野茂之, 荒勝俊, 江口泰輝, 川合修次, 佐々木大輔, 飯野久和

    栄養学雑誌   60 ( 3 )  2002

    J-GLOBAL

  • 有胞子乳酸菌と健康

    荒勝俊, 川合修次

    日本生物工学会大会講演要旨集   2001  2001

    J-GLOBAL

  • 家庭内住環境にみる真菌の動態および分布マップ作成

    高鳥浩介, 荒勝俊, 徳田一, 川合修次, 上田伸男, 秋山一男

    日本医真菌学会雑誌   42 ( Supplement 1 )  2001

    J-GLOBAL

  • 会社施設における被験者の足底への白せん菌の付着状況 社員寮とロッカー室の検討

    谷口裕子, 西岡清, 加藤卓朗, 浜正勝, 荒勝俊

    日本皮膚科学会雑誌   111 ( 3 )  2001

    J-GLOBAL

  • 家庭における細菌分布と生活者の意識・行動からみた衛生対策

    小島みゆき, 都島康彦, 小屋えな子, 荒勝俊, 川合修次, 上田伸男

    日本防菌防黴学会年次大会要旨集   28th  2001

    J-GLOBAL

  • 足白せんの実態調査 第3報 ブーツ着用女性

    加藤卓朗, 渡辺京子, 谷口裕子, 西岡清, 沖坂浩一, 荒勝俊

    日本皮膚科学会雑誌   111 ( 3 )  2001

    J-GLOBAL

  • Epidemiological Investigation of Tinea Pedis in Groups of Healthy Students, Research Workers and Females Wearing Boots.

    渡辺京子, 谷口裕子, 西岡清, 加藤卓朗, 荒勝俊, 茅根滋人

    日本医真菌学会雑誌   42 ( 4 )  2001

    J-GLOBAL

  • Isolation of Dermatophytes from Volunteers with Bare Feet in a Dormitory for Office Workers and in Locker Rooms of an Office.

    谷口裕子, 西岡清, 加藤卓朗, 浜正勝, 荒勝俊

    日本皮膚科学会雑誌   111 ( 11 )  2001

    J-GLOBAL

  • 大豆及び大豆加工食品の呈味性改善 (3) 酵素法による呈味性改善の可能性を探る

    荒勝俊

    New Food Industry   43 ( 4 )  2001

    J-GLOBAL

  • Dietary Effect of Fermented Soymilk on Lipid Metabolism and Intestinal Flora.

    荒勝俊, 大辻一也, 川合修次, 大久保一良

    日本食品科学工学会誌   48 ( 11 )  2001

    J-GLOBAL

  • 発酵食品と健康 発酵乳食品の科学 (1)

    荒勝俊

    New Food Industry   43 ( 9 )  2001

    J-GLOBAL

  • 発酵食品と健康 (2) 乳酸菌の保健効果 腸内環境改善効果

    荒勝俊

    New Food Industry   43 ( 11 )  2001

    J-GLOBAL

  • 発酵食品と健康 大豆発酵食品の科学

    荒勝俊

    New Food Industry   43 ( 8 )  2001

    J-GLOBAL

  • 長期ベッドレスト・ヘッドダウン法による腸内細胞叢などの変化

    上田伸男, 陳鋼, 渡辺高明, 荒勝俊, 海老沢秀道, 大関知子, 福岡秀興

    日本栄養・食糧学会総会講演要旨集   55th  2001

    J-GLOBAL

  • 足白せんの実態調査 その2 会社員(研究職)

    渡辺京子, 谷口裕子, 西岡清, 加藤卓朗, 荒勝俊, 茅根滋人

    日本医真菌学会雑誌   41 ( Supplement 1 )  2000

    J-GLOBAL

  • 会社社員寮における被験者の足底への白せん菌の付着状況

    谷口裕子, 西岡清, 加藤卓朗, 荒勝俊, 森啓

    日本医真菌学会雑誌   41 ( Supplement 1 )  2000

    J-GLOBAL

  • 大豆及び大豆加工食品の呈味性改善技術 1 大豆の有用性と問題点

    荒勝俊

    New Food Industry   42 ( 10 )  2000

    J-GLOBAL

  • 大豆及び大豆加工食品の呈味性改善技術 2 乳酸醗酵による呈味性改善

    荒勝俊

    New Food Industry   42 ( 12 )  2000

    J-GLOBAL

  • Alkalophilic micro-organisms and their useful enzymes.

    伊藤進, 川合修次, 小林徹, 荒勝俊, 尾崎克也

    日本生物工学会大会講演要旨集   1995  1995

    J-GLOBAL

  • Bioconcentration of n-Dodecylbenzene sulfonate in Goldfish, Carassius auratus under a Long Term Continuous Flow System.

    都島康彦, 荒勝俊, 吉村孝一

    水産増殖   43 ( 1 )  1995

    J-GLOBAL

  • 河川水中におけるLASおよび石けんの生分解性

    吉村孝一, 荒勝俊, 林克己, 川瀬次朗, 辻和郎

    陸水学雑誌   45 ( 3 )  1984

    J-GLOBAL

▼display all

Industrial Property Rights

  • 溶菌が抑制された微生物、当該微生物の製造方法、当該微生物を用いたタンパク質等の製造方法、及び微生物の溶菌抑制方法

    特許第6059416号

    荒 勝俊, 児玉 武子, 関口 順一

    Patent

    J-GLOBAL

  • σD因子抑制解除株及びそれを用いたタンパク質の製造方法

    特許第5881352号

    柴田 望, 森本 拓也, 荒 勝俊, 小笠原 直毅, 眞鍋 憲二

    Patent

    J-GLOBAL

  • 改変rRNAオペロンを有する組換え微生物

    特許第5847458号

    劉 生浩, 名取 陽祐, 影山 泰, 荒 勝俊, 河村 富士夫

    Patent

    J-GLOBAL

  • 組換え微生物を用いたタンパク質の製造方法

    特許第5828634号

    眞鍋 憲二, 児玉 武子, 荒 勝俊, 関口 順一

    Patent

    J-GLOBAL

  • 組換え枯草菌

    特許第5829802号

    眞鍋 憲二, 影山 泰, 荒 勝俊

    Patent

    J-GLOBAL

  • ポリペプチド及び組換え微生物

    特許第5806897号

    掛下 大視, 影山 泰, 荒 勝俊

    Patent

    J-GLOBAL

  • タンパク質又はポリペプチドの製造方法

    特許第5796951号

    眞鍋 憲二, 影山 泰, 荒 勝俊

    Patent

    J-GLOBAL

  • プロトプラスト形質転換効率の向上方法

    特許第5785787号

    眞鍋 憲二, 児玉 武子, 荒 勝俊, 関口 順一

    Patent

    J-GLOBAL

  • 組換え微生物

    特許第5739113号

    眞鍋 憲二, 児玉 武子, 荒 勝俊, 関口 順一

    Patent

    J-GLOBAL

  • 改変プロモーター

    特許第5735775号

    川原 彰人, 児玉 裕司, 荒 勝俊

    Patent

    J-GLOBAL

  • 遺伝子発現方法

    特許第5732209号

    眞鍋 憲二, 影山 泰, 荒 勝俊

    Patent

    J-GLOBAL

  • 新規枯草菌変異株

    特許第5695325号

    森本 拓也, 影山 泰, 荒 勝俊, 小笠原 直毅

    Patent

    J-GLOBAL

  • 宿主DNAの改変方法および選択マーカーカセット

    特許第5524492号

    荒 勝俊, 森本 拓也, 小笠原 直毅

    Patent

    J-GLOBAL

  • タンパク質又はポリペプチドの生産方法

    特許第5513759号

    劉 生浩, 荒 勝俊, 名取 陽祐, 河村 富士夫

    Patent

    J-GLOBAL

  • 置換対象領域を事前欠失させた宿主DNAの一括置換方法

    特許第5495469号

    劉 生浩, 遠藤 圭二, 荒 勝俊

    Patent

    J-GLOBAL

  • 逆位変異を利用した宿主DNAの一括置換方法

    特許第5495468号

    劉 生浩, 遠藤 圭二, 荒 勝俊

    Patent

    J-GLOBAL

  • 変異バチルス属細菌

    特許第5474448号

    河村 富士夫, 七宮 英晃, 劉 生浩, 荒 勝俊

    Patent

    J-GLOBAL

  • ビタミンK2の製造方法

    特許第5432635号

    影山 泰, 荒 勝俊

    Patent

    J-GLOBAL

  • 枯草菌変異株

    特許第5361428号

    影山 泰, 眞鍋 憲二, 荒 勝俊

    Patent

    J-GLOBAL

  • 新規枯草菌変異株及びタンパク質の製造方法

    特許第5297656号

    劉 生浩, 影山 泰, 荒 勝俊

    Patent

    J-GLOBAL

  • 改変微生物

    特許第5294673号

    荒 勝俊, 掛下 大視, 中村 幸治

    Patent

    J-GLOBAL

  • 溶菌酵素阻害剤、溶菌抑制剤及びポリ-ガンマ-グルタミン酸の分解抑制剤及びポリ-ガンマ-グルタミン酸の製造方法

    特許第5247112号

    荒 勝俊, 関口 順一, 山本 博規, 原田 宏之

    Patent

    J-GLOBAL

  • タンパク質生産方法

    特許第5164481号

    児玉 武子, 荒 勝俊, 関口 順一

    Patent

    J-GLOBAL

  • 微生物株及び目的物質の製造方法

    特許第5161507号

    影山 泰, 劉 生浩, 遠藤 圭二, 荒 勝俊

    Patent

    J-GLOBAL

  • 共凝集抑制剤

    特許第4865991号

    上村 隆明, 荒 勝俊

    Patent

    J-GLOBAL

  • 宿主微生物

    特許第4839144号

    遠藤 圭二, 劉 生浩, 荒 勝俊

    Patent

    J-GLOBAL

  • 感染防御剤

    特許第4759210号

    上村 隆明, 荒 勝俊

    Patent

    J-GLOBAL

  • 宿主DNAの欠失対象領域の欠失方法

    特許第4721868号

    劉 生浩, 遠藤 圭二, 荒 勝俊

    Patent

    J-GLOBAL

  • デオドラント剤

    特許第4723738号

    浜 正勝, 秋葉 俊一, 荒 勝俊

    Patent

    J-GLOBAL

  • シトラールアセタール

    特許第4689106号

    田中 作弥, 田中 成佳, 秋葉 俊一, 荒 勝俊, 石田 浩彦

    Patent

    J-GLOBAL

  • アメロゲニン融合タンパク質

    特許第4643932号

    林 康弘, 荒 勝俊, 斎藤 英一, 関口 浩

    Patent

    J-GLOBAL

  • 外用剤組成物

    特許第4607366号

    秋葉 俊一, 浜 正勝, 荒 勝俊, 斎藤 英一

    Patent

    J-GLOBAL

  • α-アミラーゼの生産方法

    眞鍋 憲二, 荒 勝俊

    Patent

    J-GLOBAL

  • スタテリン融合タンパク質

    特許第4564791号

    高橋 史員, 林 康弘, 秋葉 俊一, 荒 勝俊

    Patent

    J-GLOBAL

  • セルラーゼの生産方法

    影山 泰, 荒 勝俊, 朝井 計

    Patent

    J-GLOBAL

  • 化粧料

    特許第4532706号

    浜 正勝, 荒 勝俊, 森 啓, 小池 謙造, 土倉 豊樹, 西澤 義則, 境野 信, 小久保 烈王

    Patent

    J-GLOBAL

  • アポリポプロテインD分解抑制剤

    特許第4388322号

    秋葉 俊一, 荒 勝俊, 楠奥 比呂志, 西澤 義則

    Patent

    J-GLOBAL

  • p60エンドペプチダーゼ阻害剤

    荒 勝俊, 阪本 知生, 山本 博規, 針山 望, 関口 順一

    Patent

    J-GLOBAL

  • 洗浄剤組成物

    特許第4373185号

    曽禰 妙子, 登坂 正樹, 五十嵐 一暁, 荒 勝俊, 出口 勝彦

    Patent

    J-GLOBAL

  • 新規枯草菌変異株及び長寿命化した枯草菌変異株の作製方法

    児玉 武子, 門屋 亨介, 荒 勝俊, 関口 順一, 小笠原 直毅

    Patent

    J-GLOBAL

  • 細菌の溶菌抑制方法及び溶菌が抑制された細菌

    児玉 武子, 荒 勝俊, 関口 順一

    Patent

    J-GLOBAL

  • 微生物及びこれを用いたタンパク質又ポリペプチドの製造方法

    眞鍋 憲二, 荒 勝俊

    Patent

    J-GLOBAL

  • 細胞呼吸活性の測定方法及びそのキット、タンパク質生産性向上株のスクリーニング方法及びそのキット

    児玉 武子, 荒 勝俊, 関口 順一

    Patent

    J-GLOBAL

  • 皮膚疾患改善剤

    特許第4204096号

    荒 勝俊, 吉松 正, 目黒 真一, 長谷 正, 時光 一郎

    Patent

    J-GLOBAL

  • 腸内ビフィズス菌生育促進剤

    特許第4201401号

    吉松 正, 荒 勝俊

    Patent

    J-GLOBAL

  • 微生物採取方法

    特許第4111747号

    矢納 義高, 山城 高久, 芽根 滋人, 上村 隆明, 荒 勝俊

    Patent

    J-GLOBAL

  • セルラーゼ部分配列を有する融合タンパク質

    東畑 正敏, 小澤 忠弘, 遠藤 圭二, 荒 勝俊

    Patent

    J-GLOBAL

  • 腸内酪酸菌生育促進剤

    特許第3999894号

    吉松 正, 荒 勝俊, 本多 泰揮

    Patent

    J-GLOBAL

  • 組換えバチルス属細菌

    児玉 武子, 関口 順一, 遠藤 圭二, 荒 勝俊, 尾崎 克也

    Patent

    J-GLOBAL

  • 大豆発酵食品の製造方法

    特許第3824776号

    荒 勝俊, 吉松 正

    Patent

    J-GLOBAL

  • 食品の呈味改善方法

    特許第3779470号

    荒 勝俊, 吉松 正, 土屋 隆夫, 葛川 美智

    Patent

    J-GLOBAL

  • アルカリα-アミラーゼ、これを生産する微生物及び当該アルカリα-アミラーゼの製造法

    特許第3729910号

    五十嵐 一暁, 萩原 浩, 澤田 和久, 荒 勝俊, 川合 修次, 伊藤 進

    Patent

    J-GLOBAL

  • 乳酸菌含有冷凍パン

    特許第3699214号

    荒 勝俊, 滝川 博文, 森 啓, 大辻 一也

    Patent

    J-GLOBAL

  • 組換えバチルスメガテリウム菌

    林 康弘, 秋葉 俊一, 袴田 佳宏, 荒 勝俊, 斎藤 英一

    Patent

    J-GLOBAL

  • 腸内低級脂肪酸生成促進剤

    吉松 正, 荒 勝俊, 本多 泰揮

    Patent

    J-GLOBAL

  • 液化型アルカリα-アミラーゼ遺伝子

    特許第3025627号

    秦田 勇二, 尾崎 克也, 荒 勝俊, 川合 修次, 伊藤 進

    Patent

    J-GLOBAL

  • アルカリα-アミラーゼ活性を有するアルカリプルラナーゼ遺伝子

    特許第3025625号

    秦田 勇二, 五十嵐 一暁, 尾崎 克也, 荒 勝俊, 川合 修次, 伊藤 進

    Patent

    J-GLOBAL

  • 液化型アルカリα-アミラーゼ,その製造法及びこれを含有する洗浄剤組成物

    特許第2893486号

    荒 勝俊, 佐伯 勝久, 五十嵐 一暁, 高岩 美喜雄, 上村 隆明, 川合 修次, 伊藤 進, 萩原 浩, 小林 徹, 田中 篤史, 星野 栄一

    Patent

    J-GLOBAL

  • 多糖類の糖化方法

    特許第2866460号

    荒 勝俊, 佐伯 勝久, 五十嵐 一暁, 伊藤 進

    Patent

    J-GLOBAL

  • アルカリプルラナーゼ及びその製造法

    特許第2814178号

    荒 勝俊, 五十嵐 一暁, 佐伯 勝久, 川合 修次, 伊藤 進

    Patent

    J-GLOBAL

  • アルカリプルラナーゼ遺伝子を含有するDNA断片、該DNA断片を組み込んだベクター及び該ベクターを有する微生物

    特許第2814177号

    五十嵐 一暁, 荒 勝俊, 佐伯 勝久, 川合 修次, 伊藤 進

    Patent

    J-GLOBAL

  • 乳酸発酵食品及びその製造方法

    荒 勝俊, 大辻 一也

    Patent

    J-GLOBAL

  • アルカリイソアミラーゼ及びそれを生産する微生物並びに該アルカリイソアミラーゼの製造方法

    特許第2676453号

    荒 勝俊, 高岩 美喜雄, 佐伯 勝久, 五十嵐 一暁, 伊藤 進

    Patent

    J-GLOBAL

  • セルラーゼ製造法

    特許第2651570号

    荒 勝俊, 四方 資通, 吉松 正, 伊藤 進, 岡本 暉公彦

    Patent

    J-GLOBAL

  • アルカリ耐性セルラ-ゼを産生する微生物

    特許第2509537号

    川合 修次, 大越 浩美, 荒 勝俊, 伊藤 進, 岡本 暉公彦

    Patent

    J-GLOBAL

  • アルカリ耐性セルラーゼを産生する微生物

    川合 修次, 荒 勝俊, 大越 浩美, 伊藤 進, 岡本 暉公彦

    Patent

    J-GLOBAL

  • 自動食器洗浄機用洗浄剤組成物

    曽▲禰▼ 妙子, 登坂 正樹, 佐伯 勝久, 荒 勝俊, 出口 勝彦

    Patent

    J-GLOBAL

  • α-アミラーゼ活性を有する新規なアルカリプルラナーゼY、これを産生する微生物及び新規なアルカリプルラナーゼYの製造法

    荒 勝俊, 佐伯 勝久, 五十嵐 一暁, 伊藤 進

    Patent

    J-GLOBAL

  • アルカリプルラナーゼZ-1、これを生産する微生物及びアルカリプルラナーゼZ-1の製造法

    荒 勝俊, 五十嵐 一暁, 佐伯 勝久, 伊藤 進

    Patent

    J-GLOBAL

  • アルカリ耐性セルラーゼ

    川合 修次, 大越 浩美, 荒 勝俊, 伊藤 進, 岡本 暉公彦

    Patent

    J-GLOBAL

▼display all

 

Syllabus

Teaching Experience

  • 企業研究概論

    東京工業大学生命理工学部  

    2010.01
    -
    　
     

  • 生化学概論

    北海道大学大学院生化学講座  

    2010.01
    -
    　
     

  • 食品衛生概論

    宇都宮大学教育学部  

    2001.09
    -
    　
     

 

Social Activities

  • 微生物の贈り物

    くらしとバイオプラザ21  BioJapan2008 バイオカフェ 

    2008.10
    -
    　

  • 第3回松柏軒バイオカフェ 「洗剤の力～酵素の科学」

    くらしとバイオプラザ21  くらしとバイオプラザ21 

    2006.09
    -
    　

Academic Activities

  • 化学産業が紡ぐ30年後の未来社会とイノベーション戦略（電子・情報編）

    Academic research

    公益社団法人 新化学技術推進協会  

    2020.07
    -
    2021.06

  • 化学産業が紡ぐ30年後の未来社会とイノベーション戦略（水・食糧・農業編）

    Academic research

    公益社団法人 新化学技術推進協会  

    2019.07
    -
    2020.06

  • 化学産業が紡ぐ30年後の未来社会とイノベーション戦略（エネルギー・資源編）

    Academic research

    公益社団法人 新化学技術推進協会  

    2018.07
    -
    2019.06

  • 化学産業が紡ぐ30年後の未来社会とイノベーション戦略（基本戦略編）

    Academic research

    公益社団法人 新化学技術推進協会  

    2016.07
    -
    2018.06

Sub-affiliation

  • Faculty of Science and Engineering   Graduate School of Advanced Science and Engineering