Extracellular proteases produced by the wood-degrading fungus Phanerochaete chrysosporium under ligninolytic and non-ligninolytic conditions |
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Authors: | S Balachandra Dass Carlos G Dosoretz C Adinarayana Reddy Hans E Grethlein |
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Institution: | (1) Department of Microbiology and Public Health, Michigan State University, 48 824 East Lansing, MI, USA;(2) Department of Chemical Engineering, Michigan State University, 48 824 East Lansing, MI, USA;(3) NSF Center for Microbial Ecology, Michigan State University, 48 824 East Lansing, MI, USA;(4) Michigan Biotechnology Institute, 48 909 Lansing, MI, USA;(5) Present address: Division of Genetic Toxicology (HFT 120), National Center for Toxicological Research, 72079 Jefferson, AR, USA |
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Abstract: | When subjected to nitrogen limitation, the wood-degrading fungus Phanerochaete chrysosporium produces two groups of secondary metabolic, extracellular isoenzymes that depolymerize lignin in wood: lignin peroxidases and manganese peroxidases. We have shown earlier the turnover in activity of the lignin peroxidases to be due in part to extracellular proteolytic activity. This paper reports the electrophoretic characterization of two sets of acidic extracellular proteases produced by submerged cultures of P. chrysosporium. The protease activity seen on day 2 of incubation, during primary growth when nitrogen levels are not known to be limiting, consisted of at least six proteolytic bands ranging in size from 82 to 22 kDa. The activity of this primary protease was strongly reduced in the presence of SDS. Following the day 2, when nitrogen levels are known to become limiting and cultures become ligninolytic, the main protease activity (secondary protease) consisted of a major proteolytic band of 76 kDa and a minor band of 25 kDa. The major and minor secondary protease activities were inhibited by phenylmethylsulfonyl fluoride and pepstatin A, respectively. When cultures were grown in the presence of excess nitrogen (non-ligninolytic condition), the primary protease remained the principal protease throughout the culture period. These results identify and characterize a specific proteolytic activity associated with conditions that promote lignin degradation. |
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Keywords: | Extracellular fungal proteases PAGE of proteases Lignin degradation Lignin peroxidase Phanerochaete chrysosporium |
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