关键词:
溶解性多糖单加氧酶, 枯草芽孢杆菌, 信号肽, 协同效应

Abstract: In order to achieve the efficient secretion expression of lytic polysaccharide monooxygenases CBP21 in B. Subtilis, and investigate the synergistic effect of CBP21 with chitinase, this experiment constructed a series of screening vectors for signal peptides from B.subtilis. The CBP21 was cloned into Escherichia coli-Bacillus Subtilis shuttle vector pWB980, and 13 Sec-pathway signal peptides with different structure were chosen. The results showed that the signal peptide YlqB could secret the CBP21 better than the other signal peptides. The bound protein accounted for 32.39% of the total protein in supernatant, showing the highest binding activity for colloidal chitin. Furthermore, the degradation of colloidal chitin with Serratia marcescens chitinase and Aeromonas hydrophila Chi92 in the presence of CBP21 were determined. The result indicated that the addition of CBP21 could increase both the activities of S. marcescens chitinase and A. hydrophila Chi92. The activity of Chi92 was improved by 2.35 fold. Whereas for S. marcescens chitinase, CBP21 increased its activity by 1.85 fold. This study laid solid foundation for its industrial application.

Key words: lytic polysaccharide monooxygenases, Bacillus Subtilis, signal peptide, synergistic effect