Abstract
End-product inhibition by cellobiose and glucose is a rate-limiting factor in cellulose hydrolysis by cellulases. While cellobiose and glucose inhibition have been extensively investigated, cellobionate inhibition has been minimally studied despite the discovery that accessory proteins such as cellobiose dehydrogenase (CDH) work synergistically with cellulases to form aldonic acids. The fraction of equilibrated cellobionate in the cellobiono-δ-lactone form was determined by NMR over the range of pH 4–8. To better improve the understanding of cellobiono-δ-lactone and cellobionate inhibition of cellulases, we investigate the inhibition of Trichoderma reesei cellobiohydrolase I (CBHI), one of the most extensively studied CBHs, and Neurospora crassa CDH by equilibrated cellobionate. The well-characterized inhibitor cellobiose is evaluated in parallel for comparison. The mechanisms of inhibition are determined for both inhibitors and the kinetic parameters compared using a Michaelis–Menten inhibition model. Cellobiose and cellobionate inhibition of CBHI is extended to Avicel hydrolysis, along with an investigation of those inhibitors on Accelerase 1500, a commercial cellulase preparation.
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