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Partial characterization of chitinolytic enzymes from Streptomyces albidoflavus
- Broadway, R.M., Williams, D.L., Kain, W.C., Harman, G.E., Lorito, M., Ladeda, D.P.
- Letters in applied microbiology 1995 v.20 no.5 pp. 271
- Streptomyces, chitinase, O-glycoside hydrolases, beta-N-acetylhexosaminidase, enzyme activity, chitin, hydrolysis, biological control agents, fungal antagonists, antifungal properties, Fusarium oxysporum, Botrytis cinerea
- Streptomyces albidoflavus NRRL B-16746 secreted three types of chitinolytic enzymes: N-acetyl-glucosaminidase, chitobiosidase and endochitinase. Optimal activity for all three types of enzymes occurred at pH 4-6; however 55-74% of the chitobiosidase and endochitinase activity was detectable at pH 8-10. Chitobiosidase activity originated from two strongly acidic (pI < 3.0) proteins with molecular mass of 27 kDa and 34 kDa, while endochitinase activity originated from five major acidic proteins (pI 5.1, 5.3, 5.75, 5.8-5.9 and 6.4) with molecular mass of 59, 45, 38.5, 27 and 25.5 kDa. Purified chitobiosidases significantly reduced spore germination and germ tube elongation of Botrytis cinerea and Fusarium oxysporum. Chitinolytic enzymes with significant activity at pH 4-10 may be used, transgenically, to reduce the growth and/or development of a broad spectrum of insects and fungi that are major economic pests.