Enhancing the thermostability of Rhizopus oryzae lipase by combined mutation of hot-spots and engineering a disulfide bond
Author:
Affiliation:
1. Key Laboratory of Biomass Chemical Engineering of Ministry of Education
2. College of Chemical and Biological Engineering
3. Zhejiang University
4. Hangzhou 310027
5. China
6. Genclonn Biotech (Hangzhou) Co. Ltd
Abstract
The thermostability of Rhizopus oryzae lipase was greatly enhanced by combined mutation of hot-spots and engineering a disulfide bond.
Funder
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2018/RA/C8RA07767C
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1. Immobilisation and application of lipases in organic media
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3. Dietary effects of diacylglycerol rich mustard oil on lipid profile of normocholesterolemic and hypercholesterolemic rats
4. Lipase‐catalyzed interesterification reactions for human milk fat substitutes production: A review
5. Biochemical and molecular characterization of a lipase produced by Rhizopus oryzae
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