PURIFICATION AND SOME PROPERTIES OF CHITINASES FROM AEROMONAS SP NO-10S-24

Chitinases I and II were purified from the culture supernant of Aeromonas sp. 10S-24 by ammonium sulfate precipitation, SP-Sephadex C-50 chromatography, Sephacryl S-200 gel filtration, and chromatofocusing. Both enzymes were most active at pH 4.0 and the optimum temperature for I and II were 50-degrees-C and 60-degrees-C. Chitinase I was stable at pHs between 4 and 9 and at temperatures below 50-degrees-C and chitinase II was stable at pHs between 5 and 7 and at temperatures below 45-degrees-C. The molecular weights were estimated by SDS polyacrylamide gel electrophoresis to be 112,000 and 115,000 for I and II respectively, while gel filtration showed the molecular weight to be 114,000 for both types of the enzyme. The p/s for I and II were 7.9 and 8.1, respectively. The activities of both enzymes were inhibited by Ag+ and iodoacetic acid.