Display of Lignin Peroxidase on the Surface of Bacillus subtilis

Lignin peroxidase (LiP) has a good application prospect in lignin degradation, environmental treatment, straw feed, and other industries. However, its application is constrained by the high price and low stability of enzyme preparation. In this study, the Escherichia coli-Bacillus subtilis (E. coli-B. subtilis) shuttle expression vector pHS-cotG-lip was constructed and displayed on the surface of Bacillus subtilis spores. The analysis of enzymatic properties showed that the optimal catalytic temperature and pH of the immobilized LiP were 55 °C and 4.5, respectively. Compared with free LiP (42 °C and pH4.0), the optimal reaction temperature increased by 13 °C. After incubation at 70 °C for 1 h, its activity remained above 30