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Purification of a laccase from fungus combs in the nest of Odontotermes formosanus

Paper ID Volume ID Publish Year Pages File Format Full-Text
35177 45080 2010 5 PDF Available
Title
Purification of a laccase from fungus combs in the nest of Odontotermes formosanus
Abstract

A new enzyme was isolated from the fungus combs in the nest of Odontotermes formosanus and identified as a laccase. The single laccase was purified with a purification factor of 16.83 by ammonium sulphate precipitation and anion exchange chromatography, to a specific activity of 211.11 U mg−1. Its molecular mass was 65 kDa. The optimum pH value and temperature were 4.0 °C and 10 °C with ABTS as the substrate, respectively. The enzyme activity stabilized at temperatures between 10 °C and 30 °C and decreased rapidly when the temperature was above 30 °C. The Vmax and Km values were 3.62 μmol min−1 mg−1 and 119.52 μM, respectively. Ethanol concentration affected laccase activity, inhibiting 60% of enzyme activity at a concentration of 70%. Metal ions of Mg2+, Ba2+ and Fe2+ showed inhibition on enzyme activity of 17.2%, 5.3% and 9.4%, respectively, with the increase of metal ions concentration from 1 mM to 5 mM. Especially Fe2+ strongly inhibited enzyme activity up to 89% inhibition at a concentration of 1 mM.

Keywords
Fungus comb; Laccase; Odontotermes formosanus
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Purification of a laccase from fungus combs in the nest of Odontotermes formosanus
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 45, Issue 7, July 2010, Pages 1052–1056
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
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