1989•Journal of Applied BacteriologyRequires access

A note on the inhibition of cellulase binding to protein‐extracted lucerne fibre by denatured enzyme

Fred J. Stutzenberger

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Abstract

Protein‐extracted lucerne fibre rapidly bound Trichoderma reesei cellulases. The presence of denatured cellulase proteins inhibited both the binding and catalysis by active enzyme. This inhibition indicates that accumulation of denatured cellulase during repeated recycling in biomass conversion processes would progressively diminish the ability of the fibre to recover active enzyme from the product stream.

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Protein‐extracted lucerne fibre rapidly bound Trichoderma reesei cellulases. The presence of denatured cellulase proteins inhibited both the binding and catalysis by active enzyme. This inhibition indicates that accumulation of denatured cellulase during repeated recycling in biomass conversion processes would progressively diminish the ability of the fibre to recover active enzyme from the product stream.

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Available abstract

Protein‐extracted lucerne fibre rapidly bound Trichoderma reesei cellulases. The presence of denatured cellulase proteins inhibited both the binding and catalysis by active enzyme. This inhibition indicates that accumulation of denatured cellulase during repeated recycling in biomass conversion processes would progressively diminish the ability of the fibre to recover active enzyme from the product stream.

Key concepts: Cellulase, Trichoderma reesei, Enzyme, Chemistry, Biomass (ecology), Product inhibition, Biochemistry, Enzyme assay

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