Improvement of enzymatic activity of β-glucosidase from Thermotoga maritima by 1-butyl-3-methylimidazolium acetate

被引:13
作者
Kudou, Motonori [1 ]
Kubota, Yuka [2 ]
Nakashima, Nanami [1 ]
Okazaki, Fumiyoshi [1 ]
Nakashima, Kazunori [3 ]
Ogino, Chiaki [2 ]
Kondo, Akihiko [2 ]
机构
[1] Kobe Univ, Org Adv Sci & Technol, Nada Ku, Kobe, Hyogo 6578501, Japan
[2] Kobe Univ, Grad Sch Engn, Dept Chem Sci & Engn, Nada Ku, Kobe, Hyogo 6578501, Japan
[3] Tohoku Univ, Grad Sch Engn, Dept Chem Sci & Engn, Aoba Ku, Sendai, Miyagi 9808575, Japan
关键词
Ionic liquid; Cellulose; beta-Glucosidase; Enzymology; Bioprocess; IONIC LIQUIDS; TRICHODERMA-REESEI; AQUEOUS-SOLUTIONS; CELLULOSE; PRETREATMENT; STABILITY; BIOFUELS; ENZYMES; LIGNOCELLULOSE; TECHNOLOGIES;
D O I
10.1016/j.molcatb.2014.02.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The uses of ionic liquids (ILs) to alter the performance of enzymes and to pretreat cellulosic biomass have been investigated. In the present study, the activity of beta-glucosidase from Themotoga maritime (TmBgl1A) was studied in a phosphate buffer containing imidazolium-based ILs. Among the imidazolium-based ILs that were tested, 1-butyl-3-methylimidazolium acetate [Bmim][OAc] showed the most improvement for the hydrolysis activity of TmBgl1A at pH 7.0. From the steady-state emission spectra, [Bmim][OAc] quenched the intrinsic fluorescence of TmBgl1A. The improvement in the activity of TmBgl1A induced by [Bmim][OAc] could be linked to the flexibility of the conformation of TmBgl1A. (C) 2014 Elsevier B.V. All rights reserved.
引用
收藏
页码:17 / 22
页数:6
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