Formation of enzyme polymer engineered structure for laccase and cross-linked laccase aggregates stabilization

被引:45
作者
Hassani, Thanina [1 ]
Ba, Sidy [2 ]
Cabana, Hubert [1 ,3 ]
机构
[1] Univ Sherbrooke, Environm Engn Lab, Dept Civil Engn, Sherbrooke, PQ J1K 2R1, Canada
[2] Univ Sherbrooke, Dept Chem Engn, Sherbrooke, PQ J1K 2R1, Canada
[3] CHU Sherbrooke, Etienne Le Bel Clin Res Ctr, Sherbrooke, PQ J1H 5N4, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
Laccase; Cross-linked enzyme aggregates; Enzyme polymer engineered structure; Organic/inorganic surrounding network; Chitosan; IMMOBILIZED LACCASE; PLEUROTUS-OSTREATUS; WASTE-WATER; CHITOSAN; NANOPARTICLES; ELIMINATION; BIOREMEDIATION; HYDROLYSIS; SYSTEMS; SILICA;
D O I
10.1016/j.biortech.2012.10.058
中图分类号
S2 [农业工程];
学科分类号
0828 ;
摘要
Laccase and laccase-based cross-linked enzyme aggregates (CLEAs) were stabilized through the formation of a surrounding polymeric network made of chitosan and 3-aminopropyltriethoxysilane. The thermoresistance of the resulting enzyme polymer engineered structures of laccase (EPES-lac) and CLEAs (EPES-CLEA) were more than 30 times higher than that of free laccase and CLEAs at pH 3 and 40 degrees C. The EPES showed higher residual activity than the unmodified biocatalysts against chaotropic salts (up to 10 times), EDTA (up to 5 times), methanol (up to 15 times) and acetone (up to 20 times). The Michaelis-Menten kinetic parameters revealed that the affinity for 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) has doubled for the EPES-lac and EPES CLEA compared to their unmodified forms. The EPES-lac structures acted optimally at pH 4 and their activity was nearly temperature-independent, while the laccase activity of EPES-CLEA was optimal at pH 4 and 60 degrees C. Globally, the EPES have shown significantly improved properties which make them attractive candidate for the development of laccase-based applications. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:640 / 645
页数:6
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