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Purification, kinetics and spectral characterisation of a new versatile peroxidase from a Bjerkandera sp. isolate

Paper ID Volume ID Publish Year Pages File Format Full-Text
18555 42726 2006 6 PDF Available
Title
Purification, kinetics and spectral characterisation of a new versatile peroxidase from a Bjerkandera sp. isolate
Abstract

From the extracellular fluid of a novel strain of Bjerkandera sp., it was isolated, purified and identified the main enzyme responsible for Remazol Brilliant Blue R dye decolourisation. Such an enzyme is able to oxidise manganese, as well as veratryl alcohol and 2,6-dimethoxyphenol in manganese-independent reactions; hence, it can be included in the new group of versatile peroxidases. The molecular mass of said enzyme is ca. 45 kDa, and the N-terminal amino acid sequence obtained by Edman degradation is VAXPDGVNTA. The enzyme substrate range for oxidation of several phenolic and non-phenolic aromatic compounds was determined and the corresponding Michaelis–Menten kinetic constants calculated. Furthermore, spectrophotometric assays showing the Soret band and allowing observation of band shifts of the enzyme led to the conclusion that Bjerkandera strains may also synthesise at least two different versatile peroxidases, as happens with Pleurotus eryngii.

Keywords
Enzyme; Oxidoreductase; White-rot fungus
First Page Preview
Purification, kinetics and spectral characterisation of a new versatile peroxidase from a Bjerkandera sp. isolate
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 38, Issues 1–2, 3 January 2006, Pages 28–33
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering