Purification and characterization of a chitinase from Aeromonas media CZW001 as a biocatalyst for producing chitinpentaose and chitinhexaose.

Developing chitinase suitable for the bioconversion of chitin to chitin oligosaccharides has attracted significant attention due to its benefits in environmental protection. In this study, chitinase from Aeromonas media CZW001 (AmChi) was purified and characterized. The molecular weight of AmChi was approximately 40 kDa. AmChi exhibited maximum catalytic activity at pH 8.0 with an optimum temperature of 55°C and showed broad stability between 15 and 65°C and between pH 5.0 and 9.0. AmChi was activated by Mg2+ , Na+ , and K+ and inhibited by Hg+ , Co2+ , Fe2+ , Ca2+ , Ag+ , Zn2+ , and EDTA. The main products of AmChi on colloidal chitin were chitinhexaose and chitinpentaose. AmChi had better substrate specificity for powdered chitin than colloidal chitin and had a higher catalytic efficiency toward (GlcNAc)5 than colloidal chitin. AmChi inhibited fungal growth in a dose-dependent manner. These results suggest that AmChi could be used for the enzymatic degradation of chitin to produce chitinhexaose and chitinpentaose, which have several industrial applications.