Bacillus subtiis의 mannanase에 의한갈락토만난과 만노올리고당의 가수분해
Hydrolysis of Galactomannan and Manno-oligosaccharides by A Bacillus subtiis Mannanase.
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Abstract
Hydrolysis of manno-oligosaccharides and galactomannan was studied with the purified Bacillus subtilis WL-7 mannanase from recombinant Escherichia coli. The predominant products of hydrolysis were mannose, mannobiose and mannotriose. The enzyme could hydrolyze b-1,4-linked manno-oligosaccharides larger than mannobiose, but was not active on mannobiose. When the mannanase hydrolyzed manno-oligosaccharides of degree of polymerization(DP) 4-6, it was more active on the substrate of higher DP. Based on analysis of transient reaction products by TLC, the enzyme was found to have a preference for internal b-1,4-mannosidic linkages, which are the central mannosidic bond of mannotetraose and the two middle mannosidic bonds of mannopentaose. The b-1,4-mannosidic bonds situated at the second and fourth positions from the nonreducing end of mannohexaose were preferentially hydrolyzed by the mannanase. Locust bean gum(LBG) was enzymatically hydrolyzed with higher efficiency than guar gum, resulting that amount of reducing sugars was liberated more efficiently from LBG than guar gum with same activity of mannanase.
참고문헌 (18)
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