Xylogone sphaerospora 유래 정제 β-Mannanase에 의한 Picea abies Galactosyl Glucomannan 가수분해물의 중합도별 Bifidobacterium spp. 생육활성 비교

β-Mannanase from Xylogone sphaerospora was purified by Sephadex G-100 column chromatography. The specific activity of the purified enzyme was 8.24 units/mL protein, representing an 58.86-fold 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. Picea abies galactosyl glucomannan was hydrolyzed by the purified β-mannanase, and then the hydrolysates were separated by activated carbon column chromatography. The main hydrolysates were composed of D.P. (degree of polymerization) 7, 8, 12, and 13 galactosyl glucomanno-oligosaccharides. To investigate the effects of Picea abies galactosyl glucomanno-oligosaccharides on the in vitro growth of Bifidobacterium longum, B. bifidum, B. animalis, B. breve, B. infantis, B. adolescentis, and B. auglutum, Bifidobacterium spp. were cultivated individually on a modified-MRS medium containing a carbon source such as D.P. 7, 8, 12, and 13 galactosyl glucomanno-oligosaccharides. B. longum propagated 10.83-fold, 12.50-fold, 10.25- fold, and 9.25-fold more effectively by the treatment of D.P. 7, 8, 12, and 13 galactosyl glucomanno-oligosaccharides, respectively, compared to those of standard MRS medium. Especially, all four sorts of galactosyl glucomannooligosaccharides were more effective in promoting the growth of B. longum than B. animalis, B. bifidum, B. breve, and B. infantis.