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  1. 原著論文

A single mutation Asp43Arg was increased 2.5-fold the catalytic activity and maintained the stability of cold-adapted endo-1,4-beta glucanase (Ef-EG2) from Eisenia fetida

https://repo.qst.go.jp/records/2000584
https://repo.qst.go.jp/records/2000584
ffa39303-fe9a-40fd-ac10-e31ea1c89bfb
アイテムタイプ 学術雑誌論文 / Journal Article(1)
公開日 2024-08-09
タイトル
タイトル A single mutation Asp43Arg was increased 2.5-fold the catalytic activity and maintained the stability of cold-adapted endo-1,4-beta glucanase (Ef-EG2) from Eisenia fetida
言語 en
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
著者 Kuroki Chikako

× Kuroki Chikako

Kuroki Chikako

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Hirano Yuu

× Hirano Yuu

Hirano Yuu

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Nakazawa Mami

× Nakazawa Mami

Nakazawa Mami

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Sakamoto Tatsuji

× Sakamoto Tatsuji

Sakamoto Tatsuji

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Tamada Taro

× Tamada Taro

Tamada Taro

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Ueda Mitsuhiro

× Ueda Mitsuhiro

Ueda Mitsuhiro

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抄録
内容記述タイプ Abstract
内容記述 To improve the specific activity at low temperatures of Ef-EG2 and to maintain thermostability, five mutant enzymes (K273R, N372D, Q387E, N402D, D43R) were produced. The two mutant enzymes (K273R, N402D) lost the cellulase activity. The specific activities of mutant N372D, Q387E, and D43R enzymes were 2.5-fold higher than that of WT enzyme over various temperatures. The denaturation temperatures (Tm) of WT and N372D, Q387E, and D43R enzymes were 55.1℃, 51.5℃, 51.2℃, and 55.6℃. D43R showed almost the same thermostability as the WT enzyme. The three-dimensional structure of D43R was not significantly different from that of the WT enzyme, but the D43R enzyme lost the ability to bind sodium ions. D43R was introduced the additional electrostatic interaction with Asp55.
書誌情報 Current Research in Biotechnology

巻 5, p. 100126, 発行日 2023-04
出版者
出版者 Elsevier
ISSN
収録物識別子タイプ ISSN
収録物識別子 2590-2628
DOI
識別子タイプ DOI
関連識別子 10.1016/j.crbiot.2023.100126
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