Immobilization of alkaline polygalacturonate lyase from Bacillus subtilis on the surface of bacterial polyhydroxyalkanoate nano-granules

摘要: Alkaline polygalacturonate lyase (PGL), one of the pectinolytic enzymes, has been widely used for bioscouring cotton fibers, biodegumming, and biopulp production. In our study, PGL from Bacillus subtilis was successfully immobilized on surface polyhydroxyalkanoate (PHA) nanogranules by fusing to N-terminal PHA synthase Ralstonia eutropha via a designed linker. The PGL-decorated beads could be simply achieved recombinant fermentation consequent centrifugation. fused occupied 0.985% total weight purified granules, which identified mass spectrometer-based quantitative proteomics. activity (184.67 U/mg protein) little lower than that free (215.93 U/mg protein). immobilization process did not affect optimal pH temperature PGL, but it enhance thermostability as well stability at certain conditions, will extend practicability PGL-PHA in alkaline generally harsh process. Furthermore, still retained more 60% its initial after 8 cycles reuse. Our study provided novel promising approach cost-efficient vivo immobilization, contributing wider commercialization this environmental-friendly biocatalyst.