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KMID : 0903520080510030159
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
2008 Volume.51 No. 3 p.159 ~ p.163
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Purification of Xylogone sphaerospora β-mannanase and Growth Activity of Bifidobacterium spp. by Konjac Glucomannan Hydrolysates
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Lee Hee-Jung
Park Gwi-Gun
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Abstract
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Xylogone sphaerospora β-mannanase was purified by Sephadex G-100 column chromatography. The specific activity of the purified enzyme was 8.44 units/ml protein, representing an 56.27-folds purification of the original crude extract. The final preparation thus obtained showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight was determined to be 42 kDa. Konjac glucomannan was hydrolyzed by the purified β-mannanase, and then the hydrolysates was separated by activated carbon column chromatography. The main hydrolysates were composed of D.P. (Degree of Polymerization) 3 and 4 glucomannooligosaccharides. For elucidate the structure of D.P 3 and 4 glucomannooligosaccharides, sequential enzymatic action was performed. D.P 3 and 4 were identified as M-G-M and M-M-G-M (G- and M- represent glucosidic and mannosidic linkages). To investigate the effects of konjac glucomannooligosaccharides on in vitro growth of Bifidobacterium longum, B. bifidum, B. infantis, B. adolescentis, B. animalis, B. auglutum and B. breve. Bifidobacterium spp. were cultivated individually on the modified-MRS medium containing carbon source such as D.P. 3 and D.P. 4 glucomannooligosaccharides, respectively. B. longum and B. bifidum grew up 3.9-fold and 2.8-fold more effectively by the treatment of D.P. 4 glucomannooligosaccharides, compared to those of standard MRS medium. Especially, D.P. 4 was more effective than D.P. 3 glucomannooligosaccharide on the growth of Bifidobacterium spp.
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KEYWORD
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Bifidobacterium spp., β-mannanase, Konjac glucomannan
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