Bioconversion of α-Chitin by a Lytic Polysaccharide Monooxygenase Os LPMO10A Coupled with Chitinases and the Synergistic Mechanism Analysis.

The whole enzymatic conversion of chitin is a green and promising alternative to current strategies, which are based on lytic polysaccharide monooxygenases (LPMOs) and chitinases. However, the lack of LPMOs with high activity toward α-chitin limits the efficient bioconversion of α-chitin. Herein, we characterized a high chitin-active LPMO from Oceanobacillus sp. J11TS1 ( Os LPMO10A), which could promote the decrystallization of the α-chitin surface. Furthermore, when coupled with Os LPMO10A, the conversion rate of α-chitin to N -acetyl chitobiose [(GlcNAc) 2 ] by three chitinases ( Serratia marcescens , ChiA, -B, and -C) reached 30.86%, which was 2.03-folds that without the addition of Os LPMO10A. Moreover, the results of synergistic reactions indicated that Os LPMO10A and chitinases promoted the degradation of α-chitin each other mainly on the surface. To the best of our knowledge, this study achieved the highest yield of N -acetyl chitooligosaccharides ( N -acetyl COSs) among reported LPMOs-driven bioconversion systems, which could be regarded as a promising candidate for α-chitin bioconversion.