Purification and some properties of six chitinases from Aeromonas sp. no. 10S-24

Abstract

Six chitinases were purified from a culture supernatant of Aeromonas sp. no. 10S-24 by ammonium sulfate precipitation, DEAE-Sephadex A-50, Butyl-Toyopearl 650M, and chromatofocusing. These enzymes were most active at pH 3.5-4.5 and the optimum temperature were 50 degrees C. The molecular weights of the enzymes were 89,000 to 120,000 from SDS-polyacrylamide gel electrophoresis. N-Terminal amino acid sequences of the enzymes were similar to that of chitinase I.