期刊
BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
卷 15, 期 2, 页码 199-207出版社
KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
DOI: 10.1007/s12257-009-0173-1
关键词
Serratia marcescence; lipase; enzyme immobilization; chitosan; stirred-tank reactor; (-)-MPGM; isopropyl ether
资金
- National Natural Science Foundation of China [20506037]
- Ministry of Science and Technology, P.R. China [2007AA02Z225]
- National Special Fund for State Key Laboratory of Bioreactor Engineering [2060204]
The lipase from Serratia inarcescence ECU1010 (SmI) was capable of enantioselectively catalyzing the synthesis of many chiral drug precursors. This paper investigated the immobilization of Sml on appropriate supporting materials and its performance in bioreactor. Chitosan, Celite 545, and DEAE-cellulose were found to be the ideal supports among 8 carriers tested with respect to enzyme load and activity recovery of lipase. When Sml was immobilized, significant improvements of stability against pH, thermal, and operational deactivation were observed with all the 3 better supports, and the best stability was observed when the lipase was immobilized on glutaraldehyde activated chitosan. As for the effect of organic solvent in the biphasic reaction system, the hydrolytic activity of the immobilized lipase on trans-3-(4'methoxyphenyl)glycidic acid methyl ester ((+/-)-MPGM) observed in isopropyl ether was 6 and 3 times higher than those in toluene and methyl tert-butyl ether. The lipase-catalyzed production of ()-MPGM by enzymatic resolution of (+/-)-MPGM with chitosan-Sml in isopropyl ether-water biphasic system was carried out in a 2 L stirred-tank reactor. The batch operation was more efficient operation mode for the enantioselective hydrolysis of (+/-)-MPGM, affording enantiopure (+/-)-MPGM in 44.3% overall yield, in contrast to 29.3% in a continuous reactor.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据