Hostname: page-component-848d4c4894-2pzkn Total loading time: 0 Render date: 2024-06-09T11:08:24.323Z Has data issue: false hasContentIssue false

Molecular clustering of Pycnoporus strains from various geographic origins and isolation of monokaryotic strains for laccase hyperproduction

Published online by Cambridge University Press:  03 December 2002

Anne LOMASCOLO
Affiliation:
Institut de la Recherche Agronomique (INRA), Unité de Biotechnologie des Champignons Filamenteux, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Jean-Luc CAYOL
Affiliation:
Unité IRD des Bactéries Extrêmophiles UR 101, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Marjolaine ROCHE
Affiliation:
Institut de la Recherche Agronomique (INRA), Unité de Biotechnologie des Champignons Filamenteux, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Lin GUO
Affiliation:
Systematic Mycology and Lichenology Laboratory, Institute of Microbiology, Chinese Academy of Sciences, P.O. Box 2714, Beijing 100080, People's Republic of China.
Jean-Luc ROBERT
Affiliation:
Institut de la Recherche Agronomique (INRA), Unité de Biotechnologie des Champignons Filamenteux, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Eric RECORD
Affiliation:
Institut de la Recherche Agronomique (INRA), Unité de Biotechnologie des Champignons Filamenteux, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Laurence LESAGE-MEESSEN
Affiliation:
Institut de la Recherche Agronomique (INRA), Unité de Biotechnologie des Champignons Filamenteux, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Bernard OLLIVIER
Affiliation:
Unité IRD des Bactéries Extrêmophiles UR 101, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Jean-Claude SIGOILLOT
Affiliation:
Institut de la Recherche Agronomique (INRA), Unité de Biotechnologie des Champignons Filamenteux, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Marcel ASTHER
Affiliation:
Institut de la Recherche Agronomique (INRA), Unité de Biotechnologie des Champignons Filamenteux, IFR 86 de Biotechnologie Agro-Industrielle de Marseille, ESIL, Universités de Provence et de la Méditerranée, 163 Avenue de Luminy, Case 925, 13288 Marseille Cedex 09, France.
Get access

Abstract

The production of laccase, an enzyme of industrial interest, was screened among species of the genus Pycnoporus, in particular P. sanguineus. Strains were isolated from various tropical Chinese environments and phylogenetically compared to ones deposited in international collections. Molecular clustering, based on ribosomal ITS1-5.8S-ITS2 genomic sequence analysis, showed that the Chinese strains of P. sanguineus formed an homogeneous phylogenetic group distinguished by its laccase-overproducing character. The dikaryotic strain P. sanguineus G05 was selected for its ability to produce up to 40 000 U l−1 laccase in the presence of 2,5-xylidine, Tween 80 and maize bran. Since fruit bodies of P. sanguineus could be formed in the laboratory, monokaryotic laccase-hyperproducing strains were isolated using classic genetical methods. Among these isolates, strain G05.10 synthesized up to 71 000 U l−1 laccase, with a productivity of 5069 U l−1 d−1. The laccase was purified and identified as a 70 kDa protein with an acidic pI, and was very stable at high temperatures.

Type
Research Article
Copyright
© The British Mycological Society 2002

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)