Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22.

ABSTRACT: In the presented research the extracellular chitinase of Stenotrophomonas rhizophila G22 was biochemically and molecularly characterized. The studied enzyme was purified from a 72-h bacterial culture about 14 times, with a recovery of 63%. The molecular weight of the purified protein was estimated at 50 kDa by SDS-PAGE. The enzyme showed high activity against colloidal chitin. Significantly lower activities were observed with native chitin powder and chitosan. Adsorption of the enzyme to colloidal chitin and to powdered chitin at the level of 75% and 37%, respectively, was observed after 30 min of reaction. Optimum temperature and pH were 37 °C and 5.9, respectively. The enzyme demonstrated higher activity against nitrophenyl-β d N, N', N″-triacetylchitotriose a

SUBMITTER: Jankiewicz U 

PROVIDER: S-EPMC6904715 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature