Apparent cellulase activity of purified xylanase is due to contamination of assay substrate with xylan |
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| Authors: | J C Royer J S Novak J P Nakas |
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| Institution: | (1) Present address: Biology Department, Stanford University, 94305 Palo Alto, CA, USA;(2) College of Environmental Science and Forestry, State University of New York, 13210 Syracuse, NY, USA |
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| Abstract: | Summary Purified xylanase A ofTrichoderma longibrachiatum was active on one of two carboxymethyl cellulose (CMC) preparations used as cellulase assay substrates. The pattern of enzyme activity, and analysis of the substrate by acid hydrolysis and thin-layer chromatography (TLC) suggested that the enzyme had acted on xylan present in the CMC. |
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