Enzymic properties of β-mannanase from Polyporus versicolor |
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Authors: | K G Johnson and N W Ross |
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Institution: | Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada |
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Abstract: | Substrate specificities and the kinetic parameters, Km and Vmax, of the four multiple enzyme forms of extracellular β-mannanase activity purified from Polyporus versicolor were determined. Although Km values were significantly greater than those encountered in other β-mannanase systems Vmax values were equivalent or much greater, rendering the physiological efficiencies of the β-mannanase comparable to those of other β-mannanases. All enzymes preferred glucomannan as substrate, were highly refractory at low concentrations to n-octylglucopyranoside, sodium deoxylcholate, and sodium dodecylsulfate, and were largely insensitive to methanol, ethanol, acetonitrile, and dimethylsulfoxide. |
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Keywords: | β-Mannanase pulp bleachability glucomannan enzyme kinetics |
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