Synergism in binary mixtures of Thermobifida fusca cellulases Cel6B,Cel9A,and Cel5A on BMCC and Avicel |
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Authors: | Watson Donna L Wilson David B Walker Larry P |
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Institution: | (1) Department of Agricultural and Biological Engineering, Cornell University, 232 Riley-Robb Hall, 14853 Ithaca, NY;(2) Department of Molecular Biology and Genetics, Cornell University, 232 Riley-Robb Hall, 14853 Ithaca, NY;(3) Department of Biological and Environmental Engineering, Cornell University, 232 Riley-Robb Hall, 14853 Ithaca, NY |
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Abstract: | In an earlier binding study conducted in our laboratory using Thermobifida fusca cellulases Cel6B, Cel9A, and Cel5A (formally Thermomonospora fusca E3, E4, and E5), it was observed that binding capacities for these three cellulases were 18–30 times higher on BMCC than on Avicel. These
results stimulated an interest in how the difference in accessibility between the two cellulosic substrates would affect synergism
observed with cellulase mixtures. To explore the impact of substrate, accessibility on the extent of conversion and synergism,
three binary T. fusca cellulase mixtures were tested over a range of cellulase ratios and total molar cellulase concentrations on Avicel and BMCC.
Higher extents of conversion were observed for BMCC due to the higher enzyme to substrate ratio resulting from the higher
binding The processive endoglucanase, Cel9A, had four times the extent of conversion of the end endocellulase Cel5A, while
the exocellulase Cel6B had three times the extent of conversion of Cel5A. Approximately 500 nmol/g of the cel9A+Cel6B mixture
was needed to obtain 80% conversion, while the Cel6B+Cel5A and Cel9A+Cel5A mixtures required 1500 and 1250 nmol/g, respectively,
to obtain 80% conversion. Thus, it appears that the more accessible structure of BMCC, as reflected by its binding capacity,
results in relative higher processive activity. |
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Keywords: | Cellulases Thermobifida fusca synergism Avicel BMCC |
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