A Comparison of the Resolution of Selective (+/-)-Glycidyl Butyrate by Using Free and Nano-SiO2 Immobilized Porcine Pancreatic Lipase
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Published:2020-10-01
Issue:10
Volume:20
Page:6168-6172
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ISSN:1533-4880
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Container-title:Journal of Nanoscience and Nanotechnology
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language:en
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Short-container-title:j nanosci nanotechnol
Author:
Zhang Qiongdan1,
Qian Junqing1,
Guo Hui1,
Zhang Wei1,
Kuang Chunlan1
Affiliation:
1. The College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310014, PR China
Abstract
To explore the hydrolyzed properties of nano-SiO2 immobilized porcine pancreatic lipase, the selective hydrolysis of immobilized lipase for glycidyl butyrate was compared with the free enzyme. The hydrolysis selectivity of the immobilized biocatalyst was evaluated and compared
with the free enzyme using the enantiomeric excess (ee) of resolving racemic glycidyl butyrate as the indicator. The enantiomeric excess of the immobilized biocatalyst could be increased by 4.5%–10.0% which compared with the free enzyme under every single technological condition. The
ee was improved from 84.7% for free enzyme to 91.6% for the immobilized enzyme with 61.2% conversion. Compared with free enzyme, the conversion rate of the immobilized enzyme was increased slightly, but the % enantiomeric excess of the immobilized enzyme was increased greatly.
Publisher
American Scientific Publishers
Subject
Condensed Matter Physics,General Materials Science,Biomedical Engineering,General Chemistry,Bioengineering