Complete saccharification of β-glucan using hyperthermophilic endocellulase and β-glucosidase from pyrococcus furiosus

Abstract

Hyperthermophilic cellulase is an industrially important enzyme for biomass saccharification at high temperature. Two hyperthermophilic cellulases from the hyperthermophile Pyrococcus furiosus, endocellulase (EGPf) and ß-glucosidase (BGLPf), exhibit optimal activity at 90-105 °C and a combination of two enzymes can hydrolyze a wide range of ß-linked substrates. EGPf cleaves the ß(1 →4) bond of various substrates containing either only the ß(1→4) linkage or ß(1 →3),(1→4) mixed-linkages. In contrast, BGLPf preferentially hydrolyzes the ß(1→3) linkage over the ß(1→4) linkage of disaccharides. ß-Glucans are polysaccharides of D-glucose monomers formed by ß(1→3),(1→4) mixed-linkage bonds. They occur most commonly as cellulose in plants, in the bran of cereal grains, the cell wall of baker's yeast, and in certain fungi, mushrooms, and bacteria. We reveal that ß-glucan can be completely degraded to glucose at high temperature with a combination of EGPf and BGLPf.