Unfolding and refolding of GH19 chitinase Chi19MK with antifungal activity from Lysobacter sp. MK9-1 at low pH and high temperature.

The GH19 chitinase Chi19MK from Lysobacter sp. MK9-1 inhibits fungal growth. In this study, the thermal stability of Chi19MK was investigated in buffers of different pH.

GH-16 Type β-1,3-Glucanase from sp. MK9-1 Enhances Antifungal Activity of GH-19 Type Chitinase, and Its Glucan-binding Domain Binds to Fungal Cell-wall.

The GH-16 type β-1,3-glucanase (BgluC16MK) gene of sp. MK9-1 was cloned to study its antifungal activities. BgluC16MK displays amino acid sequence similarity with GluC from strain N4-7.

Cloning, expression, and characterization of a GH 19-type chitinase with antifungal activity from Lysobacter sp. MK9-1.

The chitin-assimilating gram-negative bacterium, Lysobacter sp. MK9-1, was isolated from soil and was the source of a glycoside hydrolase family 19-type chitinase (Chi19MK) gene that is 933-bp long and encodes a 311-residue protein. The deduced amino acid sequence of Chi19MK includes a signal peptide, an uncharacterized sequence, a carbohydrate-binding module family 12-type chitin binding domain, and a catalytic domain.