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.
Mukherjee
G
G
Division of Microbiology, School of Life Sciences, Visva-Bharati (Central University), Santiniketan, 731235, India.
Sen
S K
SK
D000935:Antifungal Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D002686:Chitin / Q000378:metabolism; D002688:Chitinases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D005658:Fungi / Q000187:drug effects / Q000254:growth & development; D006863:Hydrogen-Ion Concentration; D013302:Streptomyces / Q000201:enzymology*; D013696:Temperature
D000935:Antifungal Agents; D002686:Chitin; D002688:Chitinases