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Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.
Suzuki, Manami; Takita, Teisuke; Kuwata, Kohei; Nakatani, Kota; Li, Tongyang; Katano, Yuta; Kojima, Kenji; Mizutani, Kimihiko; Mikami, Bunzo; Yatsunami, Rie; Nakamura, Satoshi; Yasukawa, Kiyoshi.
Afiliação
  • Suzuki M; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
  • Takita T; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
  • Kuwata K; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
  • Nakatani K; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
  • Li T; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
  • Katano Y; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
  • Kojima K; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
  • Mizutani K; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
  • Mikami B; Research Institute for Sustainable Humanosphere, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
  • Yatsunami R; Institute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
  • Nakamura S; Department of Life Science and Technology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
  • Yasukawa K; Department of Life Science and Technology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
Biosci Biotechnol Biochem ; 85(2): 386-390, 2021 Feb 18.
Article em En | MEDLINE | ID: mdl-33604642
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Temperatura / Bacillus / Endo-1,4-beta-Xilanases / Proteínas Mutantes / Mutação Idioma: En Revista: Biosci Biotechnol Biochem Assunto da revista: BIOQUIMICA / BIOTECNOLOGIA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Japão
Texto completo
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PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Temperatura / Bacillus / Endo-1,4-beta-Xilanases / Proteínas Mutantes / Mutação Idioma: En Revista: Biosci Biotechnol Biochem Assunto da revista: BIOQUIMICA / BIOTECNOLOGIA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Japão