fulltext.study @t Gmail

Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010

Paper ID Volume ID Publish Year Pages File Format Full-Text
35845 45110 2008 8 PDF Available
Title
Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010
Abstract

An extracellular lipase was purified to homogeneity with a purification factor of 5.5-fold from a bacterial strain Serratia marcescens ECU1010. The purified lipase is a dimer with two homologous subunits, of which the molecular mass is 65 kDa, and the pI is 4.2. The pH and temperature optima were shown to be pH 8.0 and 45 °C, respectively. Among p-nitrophenyl esters of fatty acids with varied chain length, the lipase showed the maximum activity on p-nitrophenyl myristate (C14). The lipase was activated by some surfactants such as Gum Arabic, polyvinyl alcohol (PVA) and Pg350me, but not by Ca2+. The enzyme displayed pretty high stability in many water miscible and immiscible solvents. This is a unique property of the enzyme which makes it extremely suitable for chemo-enzymatic applications in non-aqueous phase organic synthesis including enantiomeric resolution. Several typical chiral compounds were tested for kinetic resolution with this lipase, consequently giving excellent enantioselectivities (E = 83 ∼>100) for glycidyl butyrate (GB), 4-hydroxy-3-methyl-2-(2-propenyl)-2-cyclopenten-1-one acetate (HMPCA), naproxen methyl ester (NME) and trans-3-(4′-methoxyphenyl) glycidic acid methyl ester (MPGM).

Keywords
Lipase; Serratia marcescens; Organic solvent tolerance; Enantiomeric resolution; Chiral compounds; Biochemical properties
First Page Preview
Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 6, June 2008, Pages 626–633
Authors
, , , , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering