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Extracellular Laccases from Cerrena unicolor 059, Cerrena unicolor 0784, and Pleurotus oastreatus 0432: A Comparative Assay

Extracellular Laccases from Cerrena unicolor 059, Cerrena unicolor 0784, and Pleurotus oastreatus... Laccases of the basidiomycetes Cerrena unicolor 059, C. unicolor 0784, and Pleurotus oastreatus 0432 were subjected to a comparative study. The enzymes were isolated as homogeneous preparations with molecular weights of 55, 56, and 57 kD, respectively. The three enzymes were found to be glycoproteins. The carbohydrate moiety of the glycoproteins included mannose, galactose, and N-acetylglucosamine. The carbohydrate moieties of the laccases from C. unicolor 059, C. unicolor 0784, and P. oastreatus 0432 accounted for 17, 23, and 24%, respectively. The pH optima of the enzymes corresponded to 4.0, 3.75, and 5.6, respectively. Thermal stability tests (carried out at 40°C) demonstrated that the laccase of C. unicolor 0784 was characterized by the highest temperature resistance (the enzyme retained 25% activity after 172 h of incubation). The values of the Michaelis constant (K M) were determined for the reactions of oxidation of pyrocatechol, hydroquinone, and potassium ferrocyanide catalyzed by the laccases of the basidiomycetes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Extracellular Laccases from Cerrena unicolor 059, Cerrena unicolor 0784, and Pleurotus oastreatus 0432: A Comparative Assay

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References (20)

Publisher
Springer Journals
Copyright
Copyright © 2003 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Medical Microbiology; Biochemistry, general; Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1023/A:1024564300641
Publisher site
See Article on Publisher Site

Abstract

Laccases of the basidiomycetes Cerrena unicolor 059, C. unicolor 0784, and Pleurotus oastreatus 0432 were subjected to a comparative study. The enzymes were isolated as homogeneous preparations with molecular weights of 55, 56, and 57 kD, respectively. The three enzymes were found to be glycoproteins. The carbohydrate moiety of the glycoproteins included mannose, galactose, and N-acetylglucosamine. The carbohydrate moieties of the laccases from C. unicolor 059, C. unicolor 0784, and P. oastreatus 0432 accounted for 17, 23, and 24%, respectively. The pH optima of the enzymes corresponded to 4.0, 3.75, and 5.6, respectively. Thermal stability tests (carried out at 40°C) demonstrated that the laccase of C. unicolor 0784 was characterized by the highest temperature resistance (the enzyme retained 25% activity after 172 h of incubation). The values of the Michaelis constant (K M) were determined for the reactions of oxidation of pyrocatechol, hydroquinone, and potassium ferrocyanide catalyzed by the laccases of the basidiomycetes.

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Oct 17, 2004

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