Purification and characterisation of a novel chitinase from persimmon (Diospyros kaki) with antifungal activity

► The Diospyros kaki chitinase (DKC) is a monomer with a molecular mass of 29kDa. ► It has optimal activity at pH 4.5 and 60°C with broad pH and thermostability. ► Internal peptide sequences of DKC showed similarity with other plant chitinases. ► DKC can hydrolyse colloidal chitin into chito-oligosacchaarides. ► DKC exhibited antifungal activity towards pathogenic fungus Trichoderma viride. A novel chitinase from the persimmon fruit was isolated, purified and characterised in this report. The Diospyros kaki chitinase (DKC) was found to be a monomer with a molecular mass of 29kDa. It exhibited optimal activity at pH 4.5 with broad pH stability from pH 4.0–9.0. It has an optimal temperature of 60°C and thermostable up to 60°C when incubated for 30min. The internal peptide sequences of DKC showed similarity with other reported plant chitinases. It has the ability to hydrolyse colloidal chitin into chito-oligomers such as chitotriose, chitobiose and into its monomer N-acetylglucosamine. It can be used to degrade chitin waste into useful products such as chito-oligosacchaarides. DKC exhibited antifungal activity towards pathogenic fungus Trichoderma viride. Chitinases with antifungal property can be used as biocontrol agents replacing chemical fungicides.