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Purification and some properties of Mn peroxidase from Lentinula edodes

Paper ID Volume ID Publish Year Pages File Format Full-Text
36097 45120 2006 5 PDF Available
Title
Purification and some properties of Mn peroxidase from Lentinula edodes
Abstract

Two manganese peroxidase isoenzymes MnP1 and MnP2, were produced by the white-rot basidiomycete Lentinula edodes on corncob solid-state cultures under optimized conditions (12 days of incubation at 30 °C in corncob solid-state medium supplemented with 0.5% glucose and 5 mM MnSO4). The main isoenzyme, MnP2, was purified to apparent electrophoretic homogeneity by using ultrafiltration, acetone precipitation and gel filtration. MnP2 had been purified 6.76-fold with a yield of 26.6%. According to data on gel filtration chromatography and sodium dodecyl sulphate polyacrilamide gel electrophoresis (SDS-PAGE), the molecular weight of the enzyme was 44 kDa. The enzyme is a glycoprotein with 17.8% of its weight in carbohydrates. The optimum pH and temperature of purified MnP were 4.5 and 40 °C, respectively. The purified enzyme was stable in the pH range 4.5–6.0 and at temperature up to 45 °C. The KM values of MnP for hydrogen peroxide and Mn2+ were, at pH 4.5, 20.8 and 22.2 × 10−3 mM, respectively, and when compared with other MnP enzymes, it was more stable in the presence of high concentrations of H2O2.

Keywords
Manganese peroxidase; Lentinula edodes; Lignin degradation; Enzyme purification
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 5, May 2006, Pages 1203–1207
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us