RESUMEN
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.
Asunto(s)
Antifúngicos/aislamiento & purificación , Quitinasas/aislamiento & purificación , Streptomyces/enzimología , Antifúngicos/química , Antifúngicos/farmacología , Quitina/metabolismo , Quitinasas/química , Quitinasas/metabolismo , Quitinasas/farmacología , Cromatografía de Afinidad , Cromatografía por Intercambio Iónico , Hongos/efectos de los fármacos , Hongos/crecimiento & desarrollo , Concentración de Iones de Hidrógeno , TemperaturaRESUMEN
In an attempt to isolate chitinase producers from soil, a streptomycete strain was found potent using natural chitin as the substrate. Chitinolytic activity was tested directly on agar plates, also with crude enzyme. Chitinase assay showed that the isolate could produce 0.8 U/ml of the enzyme. The morphological, cultural, physiological and biochemical characters of the isolate P10 were studied, and identified as Streptomyces venezuelae P10.