Purification and characterization of two chitinases from Streptomyces albovinaceus S-22

Two chitinases, A and B, were purified from the culture supernatant of Stre ptomyces albovinaceus S-22 by ammonium sulphate fraction (80%) and Sephadex G-200 gel filtration. Both enzymes had molecular weights estimated to be 4 3 and 45 kDa by SDS polyacrylamide gel electrophoresis. The enzymes were ac tive at 40 degrees C and pH 5.6 after 120 min, and stable at temperatures b elow 40 degrees C in the absence of chitin. The purified enzyme had potenti al for cell wall lysis of fungal pathogenesis tested.