Characterization of substrate-velocity relationships for the cellulase enzyme complex from Trichoderma viride Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/1r66j401v

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  • The influence of substrate and enzyme concentration on the rate of saccharification of two defined, insoluble, cellulose substrates, Avicel and Solka-Floc, by the cellulase enzyme system of Trichoderma viride has been evaluated. Assays utilized enzyme concentrations ranging from 0.014 to 0.056 filter paper unit per mL and substrate concentrations up to 10% (w/v). Analysis by initial velocity methods found the maximum velocity of the enzyme to be nearly equivalent for the two substrates and the km for the two substrates to be of similar magnitude, i.e., 0.20% for Solka-Floc and 0.63% for Avicel (w/v). Studies utilizing relatively high substrate concentrations (greater than 15 times the Km) demonstrated that the enzyme exhibits very different apparent substrate inhibition properties for the two substrates. The rate of saccharification of Avicel at relatively high substrate concentrations was up to 35% lower than the maximum rate which was obtained at a lower substrate concentration. The Avicel concentration corresponding to the maximum rate of saccharification was dependent on enzyme concentration. In contrast to the results with Avicel, the enzyme did not exhibit substrate inhibition with the Solka-Floc substrate. Potential differences in the degree of substrate inhibition with different substrates, as reported in this paper, is particularly relevant to the experimental design of comparative studies.
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