Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop

被引：13

作者：

Annaluru, Narayana

Watanabe, Seiya

Pack, Seung Pil

Abu Saleh, Ahmed

Kodaki, Tsutomu

Makino, Keisuke ^{[1
]}

机构：

[1] Kyoto Univ, Inst Adv Energy, Uji 6110011, Japan

[2] Kyoto Univ, CREST, JST, Uji 6110011, Japan

[3] Kyoto Univ, Fac Engn, Saikyo Ku, Kyoto 6158530, Japan

[4] Kyoto Univ, Int Innovat Ctr, Sakyo Ku, Kyoto 6068501, Japan

来源：

JOURNAL OF BIOTECHNOLOGY | 2007年 / 129卷 / 04期

关键词：

thermostability; xylitol dehydrogenase; structural zinc; site-directed mutagenesis;

D O I：

10.1016/j.jbiotec.2007.02.006

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Xylitol dehydrogenase from Pichia stipitis (PsXDH) is one of the key enzymes for the bio-ethanol fermentation system from xylose. Previously, we constructed the C4 mutant (S96C/S99C/Y102C) with enhanced thermostability by introduction of structural zinc. In this study, for further improvement of PsXDH thermostability, we constructed the appropriate structural zinc-binding loop by comparison with other polyol dehydrogenase family members. A high thermostability of PsXDH was obtained by subsequent site-directed mutagenesis of the structural zinc-binding loop. The best mutant in this study (C4/F98R/E101F) showed a 10.8 degrees C higher thermal transition temperature (T-CD) and 20.8 degrees C higher half denaturation temperature (T-1/2) compared with wild-type. (c) 2007 Elsevier B.V. All rights reserved.

引用

页码：717 / 722

页数：6

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