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. / Graduation date: 1990
| Identifer | oai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/27155 |
| Date | 22 November 1989 |
| Creators | Liaw, Ean-Tun |
| Contributors | Penner, Michael H. |
| Source Sets | Oregon State University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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