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| Biosci Biotechnol Biochem 1997 Oct;61(10):1739-42 |
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Purification and characterization
of konjac glucomannan degrading enzyme from anaerobic human
intestinal bacterium, Clostridium butyricum-Clostridium beijerinckii
group.
Nakajima N, Matsuura Y.
Department of Nutritional Science, Faculty of Health and Welfare
Science, Okayama Prefectural University, Japan.
Konjac glucomannan degrading enzyme was purified to homogeneity
from the culture broth of an anaerobic human intestinal bacterium,
Clostridium butyricum-Clostridium beijerinckii group. The enzyme
was composed of a single polypeptide chain with a molecular
weight of 50,000-53,000. The enzyme was an endo-beta-mannanase
that acted specifically on the polysaccharides such as konjac
glucomannan and coffee mannan, producing exclusively their smaller
oligosaccharides and the monosaccharides. The optimal pH of
the enzyme for the hydrolysis of konjac glucomannan was around
7-8 and the enzyme was stable in rather alkaline pH range of
8-10. The enzyme reaction was activated by the addition of CaCl2
and dithiothreitol. It was suggested that the enzyme might contribute
to the decomposition of konjac glucomannan in human digestive
tract.
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