Conversion of a Rhizopus chinensis lipase into an esterase by lid swapping.

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.

journal_name

J Lipid Res

authors

Yu XW,Zhu SS,Xiao R,Xu Y

doi

10.1194/jlr.M043950

subject

Has Abstract

pub_date

2014-06-01 00:00:00

pages

1044-51

issue

6

eissn

0022-2275

issn

1539-7262

pii

jlr.M043950

journal_volume

55

pub_type

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