A novel thermostable cellulase cocktail enhances lignocellulosic bioconversion and biorefining in a broad range of pH

摘要

Lignocellulose is the most abundant biomass in nature, and the effective biorefining of them is dependent upon enzymes with high catalytic activity and stability in extreme pH and high temperatures. Due to the molecular constraints for a single enzyme, obtaining a more excellent active pH range can be more easily achievable through the simultaneous activity of two or more enzymes in a cocktail. To address this, we attempted to develop a cocktail of novel thermostable cellulases with high hydrolytic ability and stability. Two cellulases were mined, identified, cloned, and expressed from the camel rumen microbiota. The PersiCel1 demonstrated its maximum relative activity at the pH of 8, and the temperature of 60 degrees C and the PersiCel2 was optimally active at the pH of 5 and the temperature of 50 degrees C.