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Acyl migration and kinetics study of 1(3)-positional specific lipase of Rhizopus oryzae-catalyzed methanolysis of triglyceride for biodiesel production

Paper ID Volume ID Publish Year Pages File Format Full-Text
34950 45061 2010 6 PDF Available
Title
Acyl migration and kinetics study of 1(3)-positional specific lipase of Rhizopus oryzae-catalyzed methanolysis of triglyceride for biodiesel production
Abstract

The lipase of Rhizopus oryzae (R. oryzae) was reported to have 1(3)-positional specificity, but in the process of R. oryzae-catalyzed biodiesel production, the yield of biodiesel (methyl esters) could reach over 80%. Although during 1(3)-positional specific lipase-catalyzed methanolysis of triglycerides, acyl migration was thought as one of the major reasons for higher methyl ester yield, there was no further study on the mechanism exploration regarding to acyl migration. In this paper, acyl migration and the related kinetics of R. oryzae-mediated methanolysis of triolein was studied systematically. Through our study, it was revealed that during the methanolysis process, acyl migration between 2-MG and 1-MG as well as acyl migration between 1,2-DG and 1,3-DG could take place independent of enzymatic catalysis. The kinetic study showed that the acyl migration was first-order reversible reaction. Based on this finding, a two-step mechanic model including acyl migration was developed for the enzyme-mediated methanolysis for biodiesel production and it was found that the reaction included consecutive hydrolysis and esterification. Further investigation on kinetics showed that R. oryzae lipase was not restrict selectivity of 1(3)-position acyl group, but a preference of 1(3)-position over 2-position, which also contributed to the higher yield of methyl esters.

Keywords
Acyl migration; Kinetics; Rhizopus oryzae; Methanolysis; Biodiesel
First Page Preview
Acyl migration and kinetics study of 1(3)-positional specific lipase of Rhizopus oryzae-catalyzed methanolysis of triglyceride for biodiesel production
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 45, Issue 12, December 2010, Pages 1888–1893
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering