Abstract
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 1h, its activity remained above 30%, while the free LiP completely lost its activity under the same conditions. Adding Mn2+, DL-lactic acid, and PEG-4000 increased the CotG-LiP enzyme activity to 313%, 146%, and 265%, respectively. The recyclability of spore display made the fusion protein CotG-LiP retain more than 50% enzyme activity after four cycles. The excellent recycling rate indicated that LiP displayed on the spore surface had a good application prospect in sewage treatment and other fields, and also provided a reference for the rapid and low-cost immobilized production of enzyme preparations.
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