The catalytic potency of β-glucosidase from Pyrococcus furiosus in the direct glucosylation reaction

被引:5
作者
de Roode, BM
van der Meer, TD
Kaper, T
Franssen, MCR
van der Padt, A
van der Oost, J
Boom, RM
机构
[1] Univ Wageningen & Res Ctr, Organ Chem Lab, NL-6703 HB Wageningen, Netherlands
[2] Univ Wageningen & Res Ctr, Food & Bioproc Engn Grp, Dept Agrotechnol & Food Sci, NL-6703 HD Wageningen, Netherlands
[3] Univ Wageningen & Res Ctr, Microbiol Lab, Dept Biomol Sci, NL-6703 CT Wageningen, Netherlands
关键词
D O I
10.1016/S0141-0229(01)00441-0
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
Enzymes from extremophiles operate at conditions that are different from their 'normal' counterparts, and are therefore a useful extension of the enzyme toolbox. In this paper, the direct glucosylation reaction mediated by a hyperthermophilic beta -glucosidase from Pyrocuccus furiosus was investigated. Hexanol was successfully coupled to glucose with this enzyme. A preliminary study was conducted to improve the product yield. A maximum product concentration of 12.9 g.l(-1) was attainable by increasing the glucose concentration to the maximum solubility of 2000 g.(kg buffer solution)(-1) at the reaction temperature. The highest glucose based yield of 2.64% was achieved with a glucose concentration of 900 g.(kg buffer solution)(-1) at a reaction temperature of 65 degreesC and a pH of 6.0. Performing the reaction at higher pH and temperature led to lower product concentrations. This was caused by deactivation of the enzyme accompanied by browning of the reaction mixture. A pH of 4.4 did have a negative effect on both the storage and the operational stability of the enzyme. (C) 2001 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:621 / 624
页数:4
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