A new thermostable β-glucosidase mined from Dictyoglomus thermophilum: Properties and performance in octyl glucoside synthesis at high temperatures

被引:28
作者
Zou, Zheng-Zheng [1 ]
Yu, Hui-Lei [1 ]
Li, Chun-Xiu [1 ]
Zhou, Xin-Wen [2 ,3 ]
Hayashi, Chihiro [4 ]
Sun, Jie [1 ]
Liu, Bao-Hong [2 ,3 ]
Imanaka, Tadeyuki [1 ,4 ]
Xu, Jian-He [1 ]
机构
[1] E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Lab Biocatalysis & Synthet Biotechnol, Shanghai 200237, Peoples R China
[2] Fudan Univ, Dept Chem, Shanghai 200433, Peoples R China
[3] Fudan Univ, Inst Biomed Sci, Shanghai 200433, Peoples R China
[4] Ritsumeikan Univ, Coll Life Sci, Dept Biotechnol, Shiga 5258577, Japan
基金
中国国家自然科学基金;
关键词
beta-Glucosidase; Dictyoglomus thermophilum; Thermostability; Octyl glucoside; Reverse hydrolysis; D-GLUCOPYRANOSIDES; ENZYMATIC CATALYSIS; PYROCOCCUS-FURIOSUS; REVERSE HYDROLYSIS; BIPHASIC SYSTEM; APPLE SEED; GENE; PURIFICATION; EXPRESSION; ALCOHOLS;
D O I
10.1016/j.biortech.2012.04.040
中图分类号
S2 [农业工程];
学科分类号
0828 ;
摘要
A new beta-glucosidase (DtGH) representing 40% identity with an apple seed glycosidase (ASG) was cloned from Dictyoglomus thermophilum. DtGH showed extremely high thermostability in aqueous solution, with half-lives of 533, 44, and 5 h measured at 70, 80 and 90 degrees C, respectively. Therefore it was used for direct glycosylation of n-octanol at 70 degrees C instead of 50 degrees C as usually. As a result, the glucose based conversion was increased by 27%, but the time spent to reach equilibrium was decreased from 7 d to 3 d. This enzyme also exhibited excellent stability under the reaction environment, retaining 70-80% of its initial activity after 7 d of incubation at 70 degrees C in either 1.7 M glucose solution or octanol-aqueous (85:15, v/v) system. It could retain part of synthetic activity even in boiling water. Owing to the strong glucose-tolerance and extremely high thermostability, DtGH should be promising for various glucosides synthesis. Crown Copyright (c) 2012 Published by Elsevier Ltd. All rights reserved.
引用
收藏
页码:425 / 430
页数:6
相关论文
共 30 条
[1]   Microbial β-glucosidases:: Cloning, properties, and applications [J].
Bhatia, Y ;
Mishra, S ;
Bisaria, VS .
CRITICAL REVIEWS IN BIOTECHNOLOGY, 2002, 22 (04) :375-407
[2]   Mining Dictyoglomus turgidum for Enzymatically Active Carbohydrases [J].
Brumm, Phillip ;
Hermanson, Spencer ;
Hochstein, Becky ;
Boyum, Julie ;
Hermersmann, Nick ;
Gowda, Krishne ;
Mead, David .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2011, 163 (02) :205-214
[3]   The catalytic potency of β-glucosidase from Pyrococcus furiosus in the direct glucosylation reaction [J].
de Roode, BM ;
van der Meer, TD ;
Kaper, T ;
Franssen, MCR ;
van der Padt, A ;
van der Oost, J ;
Boom, RM .
ENZYME AND MICROBIAL TECHNOLOGY, 2001, 29 (10) :621-624
[4]   Sequencing, cloning, and high-level expression of the pfp gene, encoding a PPi-dependent phosphofructokinase from the extremely thermophilic eubacterium Dictyoglomus thermophilum [J].
Ding, YHR ;
Ronimus, RS ;
Morgan, HW .
JOURNAL OF BACTERIOLOGY, 2000, 182 (16) :4661-4666
[5]   Comparison between various commercial sources of almond β-glucosidase for the production of alkyl glucosides [J].
Ducret, A ;
Trani, M ;
Lortie, R .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2006, 38 (02) :91-94
[6]   Screening of various glycosidases for the synthesis of octyl glucoside [J].
Ducret, A ;
Trani, M ;
Lortie, R .
BIOTECHNOLOGY AND BIOENGINEERING, 2002, 77 (07) :752-757
[7]   Catalytical potency of beta-glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis [J].
Fischer, L ;
Bromann, R ;
Kengen, SWM ;
deVos, WM ;
Wagner, F .
BIO-TECHNOLOGY, 1996, 14 (01) :88-91
[8]   Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance [J].
Garcia-Galan, Cristina ;
Berenguer-Murcia, Angel ;
Fernandez-Lafuente, Roberto ;
Rodrigues, Rafael C. .
ADVANCED SYNTHESIS & CATALYSIS, 2011, 353 (16) :2885-2904
[9]   Sequencing and expression of a β-mannanase gene from the extreme thermophile Dictyoglomus thermophilum Rt46B.1, and characteristics of the recombinant enzyme [J].
Gibbs, MD ;
Reeves, RA ;
Sunna, A ;
Bergquist, PL .
CURRENT MICROBIOLOGY, 1999, 39 (06) :351-357
[10]   CLONING, SEQUENCING, AND EXPRESSION OF A XYLANASE GENE FROM THE EXTREME THERMOPHILE DICTYOGLOMUS-THERMOPHILUM RT46B.1 AND ACTIVITY OF THE ENZYME ON FIBER-BOUND SUBSTRATE [J].
GIBBS, MD ;
REEVES, RA ;
BERGQUIST, PL .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1995, 61 (12) :4403-4408