Characterization of a chitinase from Salinivibrio sp BAO-1801 as an antifungal activity and a biocatalyst for producing chitobiose

Salinivibrio genus is commonly found in salted seafood products. In this study, chitinase produced by Salinivibrio sp. BAO-1801 isolated from salted fermented shrimp was purified and subsequently characterized. The molecular weight of BAO-1801 chitinase was approximately 94.2kDa by SDS-PAGE analysis. It was classified as a chitinase C based on homology analysis of its N-terminal amino acid residues. This strain BAO-1801 chitinase was then used for synthesis of (GlcNAc)2. Degradation of colloidal chitin and N-acetyl chitooligosaccharides by BAO-1801 chitinase was then analyzed and (GlcNAc)2 was identified as the main product by thin layer chromatography and high-performance liquid chromatography. Effects of temperature and pH on activity and stability of BAO-1801 chitinase were also investigated. Furthermore, this enzyme inhibited fungal growth in a dose-dependent manner. Taken together, these results suggest that this Salinivibrio or its chitinase can be used for the enzymatic degradation of chitin to produce chitobiose in industrial process.