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KMID : 0364820100460040397
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Korean Journal of Microbiology
2010 Volume.46 No. 4 p.397 ~ p.400
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Mannanolytic Enzyme Activity of Paenibacillus woosongensis
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Yoon Ki-Hong
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Abstract
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The activities of mannanase, β-mannosidase, and α-galactosidase were detected in culture filtrate of Paenibacillus woosongensis showing mannanolytic activity for locust bean gum. Optimal conditions occurred at pH 5.5 and 60°C for mannanase toward locust bean gum, pH 6.5 and 50°C for β -mannosidase toward para-nitrophenyl-β-D-annopyranoside, and pH 6.0-6.5 and 50°C for α -galactosidase toward para-nitrophenyl-α-D-galactopyranoside in the culture filtrate, respectively. The mannanolytic enzyme of culture filtrate hydrolyzed mannobiose as well as manno-oligosaccharides including mannotriose, mannotetraose, mannopentaose and mannohexaose. It could also hydrolyze α-1,6 linked galacto-oligosaccharides such as melibiose, raffinose and stachyose to liberate galactose residue. From these results, it is assumed that P. woosongensis produces three enzymes required for the complete decomposition of alactomannan.
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KEYWORD
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α-galactosidase, β-mannosidase, mannanase, P. woosongensis
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