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Characterization of a spore surface lipase from the biocontrol agent Metarhizium anisopliae

Paper ID Volume ID Publish Year Pages File Format Full-Text
35480 45092 2009 6 PDF Available
Title
Characterization of a spore surface lipase from the biocontrol agent Metarhizium anisopliae
Abstract

A Metarhizium anisopliae spore surface lipase (MASSL) strongly bound to the fungal spore surface has been purified by ion exchange chromatography on DEAE sepharose followed by ultrafiltration and hydrophobic interaction chromatography on phenyl sepharose. Electrophoretic analyses showed that the molecular weight of this lipase is ∼66 kDa and pI is 5.6. Protein sequencing revealed that identified peptides in MASSL shared identity with several lipases or lipase-related sequences. The enzyme was able to hydrolyze triolein, the animal lipid cholesteryl stearate and all ρNP ester substrates tested with some preference for esters with a short acyl chain. The values of Km and Vmax for the substrates ρNP palmitate and ρNP laurate were respectively 0.474 mM and 1.093 mMol min−1 mg−1 and 0.712 mM and 5.696 mMol min−1 mg−1. The optimum temperature of the purified lipase was 30 °C and the enzyme was most stable within the most acid pH range (pH 3–6). Triton X-100 increased and SDS reduced enzyme lipolytic activity. MASSL activity was stimulated by Ca2+, Mg2+ and Co2+ and inhibited by Mn2+. The inhibitory effect on activity exerted by EDTA and EGTA was limited, while the lipase inhibitor Ebelactone B completely inhibited MASSL activity as well as PMSF. Methanol 0.5% apparently did not affect MASSL activity while β-mercaptoethanol activated the enzyme.

Keywords
Metarhizium anisopliae; Insect fungus; Spore surface lipase; Substrate specificity; Enzyme characteristics
First Page Preview
Characterization of a spore surface lipase from the biocontrol agent Metarhizium anisopliae
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 8, August 2009, Pages 829–834
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering