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An analytical method for determining relative specificities for sequential reactions catalyzed by the same enzyme: Application to the hydrolysis of triacylglycerols by lipases

Paper ID Volume ID Publish Year Pages File Format Full-Text
24810 43538 2008 8 PDF Available
Title
An analytical method for determining relative specificities for sequential reactions catalyzed by the same enzyme: Application to the hydrolysis of triacylglycerols by lipases
Abstract

We propose a model for the sequential hydrolysis of ester bonds of triacylglycerols by lipases and use it as the basis for an analytical method for determining the relative specificity of the lipase for the various substrates with which it can react, when the substrates occur simultaneously in a single reaction system. We then apply the method to our own data and literature data involving the hydrolysis of triacylglycerols by lipases. Our model is able to fit well to most of the reaction profiles, enabling the estimation of relative specificities. We discuss the limitations and potential applications of our method.

Keywords
Lipase; Mathematical model; Specificity constant; Triacylglycerol; Diacylglycerol; Monoacylglycerol; Sequential reactions
First Page Preview
An analytical method for determining relative specificities for sequential reactions catalyzed by the same enzyme: Application to the hydrolysis of triacylglycerols by lipases
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 133, Issue 3, 1 February 2008, Pages 343–350
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering