The β-glucosidase system of the thermophilic fungus Chaetomium thermophile Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/hh63t1351

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  • The thermophilic fungus Chaetomium thermophile was shown to contain three major β-glucosidases, a cell-bound cellobiase, a cellbound aryl-β-glucosidase and an extracellular aryl-β-glucosidase. The enzymes were partially purified and studied with respect to thermal stability and certain kinetic parameters. Two of the β-glucosidases are fairly stable at the maximum growth temperature of C. thermophile, while the third decays rapidly at this temperature. The aryl-β-glucosidases differ in molecular weight and thermal stability, but are strikingly similar in a number of other properties. The control of the synthesis of the β-glucosidase of C. thermophile was studied, using selective inactivation to differentiate between the enzyme activities. Cellobiase and cellulose are inducers of the cellobiase but not of the aryl-β-glucosidases. When the fungus is grown on starch medium, the activities of all three enzymes increase sharply after the exponential phase of growth. The significance of the results is discussed with respect to the possible functions of the β-glucosidases. The cellobiase of C. thermophile was purified from cellulose grown mycelia, and was homogeneous as judged by disc gel electrophoresis and sedimentation equilibrium analysis. The enzyme is a single polypeptide with a molecular weight of about 50, 000. It has a fairly large tyrosine and tryptophan content and an energy activationof 9. 4 Kcal per mole.
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