The mutation of Thr315 to Asn of GH10 xylanase XynR increases the alkaliphily but decreases the alkaline resistance.

Kuwata, Kohei; Suzuki, Manami; Takita, Teisuke; Yatsunami, Rie; Nakamura, Satoshi; Yasukawa, Kiyoshi

Kuwata, Kohei; Suzuki, Manami; Takita, Teisuke; Yatsunami, Rie; Nakamura, Satoshi; Yasukawa, Kiyoshi.

Afiliação

Kuwata K; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
Suzuki M; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
Takita T; Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
Yatsunami R; Department of Life Science and Technology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, Japan.
Nakamura S; Department of Life Science and Technology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, Japan.
Yasukawa K; National Institute of Technology, Numazu College, Ooka, Numazu, Shizuoka, Japan.

Biosci Biotechnol Biochem ; 85(8): 1853-1860, 2021 Jul 23.

Article em En | MEDLINE | ID: mdl-34077498

Assuntos

Álcalis/metabolismo; Asparagina/química; Treonina/química; Xilosidases/metabolismo; Substituição de Aminoácidos; Catálise; Estabilidade Enzimática; Concentração de Íons de Hidrogênio; Cinética; Temperatura; Xilosidases/química; Xilosidases/genética

Palavras-chave

GH10; alkaline resistance; alkaliphily; xylan; xylanase

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Asparagina / Treonina / Xilosidases / Álcalis Idioma: En Ano de publicação: 2021 Tipo de documento: Article

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