Purification, characterization, and antifungal activity of chitinase from Streptomyces venezuelae P10

Streptomyces venezuelae P-10 could produce extracellular chitinase in a medium containing 0.6% colloidal chitin that was fermented for 96 hours at 30 degrees C. The enzyme was purified to apparent homogeneity with 80% saturation of ammonium sulfate as shown by chitin affinity chromatography and DEAE-cellulose anion-exchange chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the enzyme showed a molecular weight of 66 kDa. The chitinase was characterized, and antifungal activity was observed against phytopathogens. Also, the first 15 N-terminal amino-acid residues of the chitinase were determined. The chitin hydrolysed products were N-acetylglucosamine and N, N'-diacetylchitobiose.