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 sp. J11TS1 (LPMO10A), which could promote the decrystallization of the α-chitin surface. Furthermore, when coupled with LPMO10A, the conversion rate of α-chitin to -acetyl chitobiose [(GlcNAc)] by three chitinases (, ChiA, -B, and -C) reached 30.86%, which was 2.03-folds that without the addition of LPMO10A. Moreover, the results of synergistic reactions indicated that 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 -acetyl chitooligosaccharides (-acetyl COSs) among reported LPMOs-driven bioconversion systems, which could be regarded as a promising candidate for α-chitin bioconversion.
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