Abstract
Two chitinases, A and B, were purified from the culture supernatant of Streptomyces albovinaceus S-22 by ammonium sulphate fraction (80%) and Sephadex G-200 gel filtration. Both enzymes had molecular weights estimated to be 43 and 45 kDa by SDS polyacrylamide gel electrophoresis. The enzymes were active at 40 °C and pH 5.6 after 120 min, and stable at temperatures below 40 °C in the absence of chitin. The purified enzyme had potential for cell wall lysis of fungal pathogenesis tested.
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