Conversion of a Rhizopus Chinensis Lipase into an Esterase by Lid Swapping

Overview

Journal J Lipid Res

Publisher Elsevier

Specialty Biochemistry

Date 2014 Mar 28

PMID 24670990

Citations 10

Authors

Xiao-Wei Yu

Shan-Shan Zhu

Rong Xiao

Yan Xu

Affiliations

Soon will be listed here.

Abstract

In an effort to explore the feasibility of converting a lipase into an esterase by modifying the lid region, we designed and characterized two novel Rhizopus chinensis lipase variants by lid swapping. The substrate specificity of an R. chinensis lipase was successfully modified toward water-soluble substrates, that is, turned into an esterase, by replacing the hydrophobic lid with a hydrophilic lid from ferulic acid esterase from Aspergillus niger Meanwhile, as a comparison, the lid of R. chinensis lipase was replaced by a hydrophobic lid from Rhizomucor miehei lipase, which did not alter its substrate specificity but led to a 5.4-fold higher catalytic efficiency (k*cat/K*m) toward p-nitrophenyl laurate. Based on the analysis of structure-function relationships, it suggests that the amphipathic nature of the lid is very important for the substrate specificity. This study provides new insight into the structural basis of lipase specificities and a way to tune the substrate preference of lipases.

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