1995 Volume 59 Issue 11 Pages 2162-2164
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°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.
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