文献类型：期刊文献

英文题名：Crosslinking of enzyme coaggregate with polyethyleneimine: A simple and promising method for preparing stable biocatalyst of Serratia marcescens lipase

作者：Pan, Jiang[1]; Kong, Xu-Dong[1]; Li, Chun-Xiu[1]; Ye, Qin[1]; Xu, Jian-He[1]; Imanaka, Tadayuki[1,2]

机构：[1] State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai 200237, China; [2] Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan

年份：2011

卷号：68

期号：3-4

起止页码：256

外文期刊名：Journal of Molecular Catalysis B: Enzymatic

收录：EI(收录号：20110313594724)

语种：英文

外文关键词：Coprecipitation - Enzyme immobilization

摘要：Crosslinking of enzyme aggregates is a promising method for enzyme immobilization. In this work, crosslinked enzyme coaggregates of Serratia marcescens lipase with polyethyleneimine (CLECAs-SML-PEI) were prepared using polyethyleneimine (PEI) as coprecipitant and glutaraldehyde as crosslinking reagent. The crude lipase solution at a low protein concentration (0.1 mg/ml), with PEI at a mass ratio of 3:1 (PEI/protein, w/w), was found to be most adequate for the coprecipitation of SML. After crosslinking of the coaggregate of SML-PEI with 0.2% (w/v) glutaraldehyde under ambient temperature, over 70% of the total lipase activity was recovered. Compared with the free SML, the optimum temperature of the CLECAs-SML-PEI was enhanced from 50 °C to 60 °C and its thermal stability was also significantly improved. CLECAs-SML-PEI showed excellent operational stability in repeated use in aqueous-toluene biphasic system for asymmetric hydrolysis of trans-3-(4′-methoxyphenyl) glycidic acid methyl ester (MPGM), without significant inactivation after 10 rounds of repeated use. ? 2010 Elsevier B.V. All rights reserved.