Cellulase Inhibition by High Concentrations of Monosaccharides

• Published in: Journal of agricultural and food chemistry Vol. 62; no. 17; pp. 3800 - 3805
• Main Authors: Hsieh, Chia-wen C, Cannella, David, Jørgensen, Henning, Felby, Claus, Thygesen, Lisbeth G
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 30.04.2014; American Chemical Society, Books and Journals Division
• Subjects: adsorption; beta-glucosidase; biodegradation; biomass; cellobiose; Cellulase - antagonists & inhibitors; Cellulase - chemistry; cellulose; Cellulose - chemistry; endo-1,4-beta-glucanase; Enzyme Inhibitors - chemistry; galactose; glucose; Glucose - chemistry; hydrolysis; Kinetics; mannose; Monosaccharides - chemistry; nuclear magnetic resonance spectroscopy; stereoisomers; cellulase adsorption; enzymatic hydrolysis; T2 relaxation; cellulase inhibition; water availability
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf5012962

Biological degradation of biomass on an industrial scale culminates in high concentrations of end products. It is known that the accumulation of glucose and cellobiose, end products of hydrolysis, inhibit cellulases and decrease glucose yields. Aside from these end products, however, other monosaccharides such as mannose and galactose (stereoisomers of glucose) decrease glucose yields as well. NMR relaxometry measurements showed direct correlations between the initial T2 of the liquid phase in which hydrolysis takes place and the total glucose production during cellulose hydrolysis, indicating that low free water availability contributes to cellulase inhibition. Of the hydrolytic enzymes involved, those acting on the cellulose substrate, that is, exo- and endoglucanases, were the most inhibited. The β-glucosidases were shown to be less sensitive to high monosaccharide concentrations except glucose. Protein adsorption studies showed that this inhibition effect was most likely due to catalytic, and not binding, inhibition of the cellulases.