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 94.2 kDa 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.