Laccase activities of Penicillium chrysogenum in relation to lignin degradation
An extracellular laccase capable of oxidizing ABTS (the diammonium salt of 2,2'-azinobis-3-ethylbenzothiazoline-6-sulfonic acid) was detected in ligninolytic cultures of Penicillium chrysogenum. By contrast, no lignin peroxidase, manganese-dependent peroxidase or aryl-alcohol oxidase was detect...
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| Veröffentlicht in: | Applied microbiology and biotechnology 1996, Vol.45 (3), p.399-403 |
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| container_title | Applied microbiology and biotechnology |
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| creator | Rodriguez, A Falcon, M.A Carnicero, A Perestelo, F Fuente, G. de la Trojanowski, J |
| description | An extracellular laccase capable of oxidizing ABTS (the diammonium salt of 2,2'-azinobis-3-ethylbenzothiazoline-6-sulfonic acid) was detected in ligninolytic cultures of Penicillium chrysogenum. By contrast, no lignin peroxidase, manganese-dependent peroxidase or aryl-alcohol oxidase was detected at any time during culturing. Both ABTS laccase activity and mineralization of dehydrogenative polymerizate of coniferyl alcohol were regulated by the C/N ratio in the medium and partially inhibited in the presence of thioglycolic acid, suggesting that both events are associated. In the presence of several known laccase inducers neither ABTS laccase activity nor mineralization rates were enhanced. However, a new laccase was detected in P. chrysogenum, able to oxidize 2,6-dimethoxyphenol but not involved in lignin mineralization. Studies with the known ligninolytic basidiomycete Trametes villosa suggest that lignin degradation by this fungus also involves the action of laccase. |
| doi_str_mv | 10.1007/s002530050702 |
| format | Article |
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By contrast, no lignin peroxidase, manganese-dependent peroxidase or aryl-alcohol oxidase was detected at any time during culturing. Both ABTS laccase activity and mineralization of dehydrogenative polymerizate of coniferyl alcohol were regulated by the C/N ratio in the medium and partially inhibited in the presence of thioglycolic acid, suggesting that both events are associated. In the presence of several known laccase inducers neither ABTS laccase activity nor mineralization rates were enhanced. However, a new laccase was detected in P. chrysogenum, able to oxidize 2,6-dimethoxyphenol but not involved in lignin mineralization. Studies with the known ligninolytic basidiomycete Trametes villosa suggest that lignin degradation by this fungus also involves the action of laccase.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s002530050702</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Fundamental and applied biological sciences. 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By contrast, no lignin peroxidase, manganese-dependent peroxidase or aryl-alcohol oxidase was detected at any time during culturing. Both ABTS laccase activity and mineralization of dehydrogenative polymerizate of coniferyl alcohol were regulated by the C/N ratio in the medium and partially inhibited in the presence of thioglycolic acid, suggesting that both events are associated. In the presence of several known laccase inducers neither ABTS laccase activity nor mineralization rates were enhanced. However, a new laccase was detected in P. chrysogenum, able to oxidize 2,6-dimethoxyphenol but not involved in lignin mineralization. Studies with the known ligninolytic basidiomycete Trametes villosa suggest that lignin degradation by this fungus also involves the action of laccase.</description><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Mission oriented research</topic><topic>Penicillium chrysogenum</topic><topic>Physiology and metabolism</topic><topic>soil biology</topic><topic>soil science</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rodriguez, A</creatorcontrib><creatorcontrib>Falcon, M.A</creatorcontrib><creatorcontrib>Carnicero, A</creatorcontrib><creatorcontrib>Perestelo, F</creatorcontrib><creatorcontrib>Fuente, G. de la</creatorcontrib><creatorcontrib>Trojanowski, J</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodriguez, A</au><au>Falcon, M.A</au><au>Carnicero, A</au><au>Perestelo, F</au><au>Fuente, G. de la</au><au>Trojanowski, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Laccase activities of Penicillium chrysogenum in relation to lignin degradation</atitle><jtitle>Applied microbiology and biotechnology</jtitle><date>1996</date><risdate>1996</risdate><volume>45</volume><issue>3</issue><spage>399</spage><epage>403</epage><pages>399-403</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>An extracellular laccase capable of oxidizing ABTS (the diammonium salt of 2,2'-azinobis-3-ethylbenzothiazoline-6-sulfonic acid) was detected in ligninolytic cultures of Penicillium chrysogenum. 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| subjects | Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Fundamental and applied biological sciences. Psychology Mission oriented research Penicillium chrysogenum Physiology and metabolism soil biology soil science |
| title | Laccase activities of Penicillium chrysogenum in relation to lignin degradation |
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