Fusions of Amphipathic Peptide to the Alkaline Polygalacturonate Lyase from Bacillus sp. WSHB04-02 Improves the Production

Abstract:

Alkaline polygalacturonatelyase（PGL）is one of important industrial enzymes，which was widely used in food，textile and paper industries. In this study，we constructed and expressed six Self-assembling amphipathic peptides （SAPs） ，whihch were attached to the N terminus of the PGL，to improve the secretory expression of PGL in E.coli. Finally PGL-S1 stood out with enzyme activity improving from 129.65 U/mL to 535.47 U/mL，while the otherenzyme activity weredecreased. There was no obvious change in the extracellular yield of PGL by SDS-PAGE analysis. It indicated that the high enzyme activity was caused by the improving catalytic efficiency. The Grave Value showed that the hydrophobicity of SAP1 was different with the others，which was the main interaction for the accumulation of protein to enhance the interaction between protein and substrate. It was conferred that the improving surface hydrophobicity made a big effect on the catalytic efficiency. PGL-S1has huge potential use for industrial application.