The Enzymatic Pattern of Bifdobacterium sp. Int-57 Isolated from Korean Feces

한국인 분변으로부터 분리한 Bifidobacterium sp. Int-57의 효소 Pattern

  • 박헌국 (서울대학교 식품공학과 및 농업신소재연구센터) ;
  • 강동현 (서울대학교 식품공학과 및 농업신소재연구센터) ;
  • 이계호 (서울대학교 식품공학과 및 농업신소재연구센터) ;
  • 윤석환 (서울대학교 식품공학과 및 농업신소재연구센터) ;
  • 이세경 (한림대학교 식품영양학과) ;
  • 지근억 (한림대하교 식품영양학과)
  • Published : 1992.12.01

Abstract

In order to study the physiological properties of the intestinal bacteria, we isolated the intestinal bacteria of Koreans and tested the enzymatic patterns. Isolated Bifidobacterium sp. Int-57 had the higher activity of $\alpha$-glucosidase, $\beta$-glucosidase, $\alpha$-galactosidase, $\beta$-galactosidase. $\beta$-xylosidase and $\alpha$-arabinofuranosidase than other intestinal microorganisms. The effect of the carbon sources on the production of each enzymes of Bijidobacterium sp. Int-57 was investigated. The most suitable carbon source for the production of $\beta$-glucosidase was maltose, for a-glucosidase cellobiose, for $\alpha$-galactosidase raffinose, for $\beta$-galactosidase lactose, and for $\beta$-xylosidase and $\alpha$-arabinofuranosidase xylose, respectively. In addition, we investigated the optimal conditions and pH stability of each crude enzymes. The optimal condition of a-glucosidase was pH 6.0 and $40^{\circ}C$. that of Jj-glucosidase pH 7.0 and 50oe, that of $\beta$-galactosidase pH 7.0 and $50^{\circ}C$, that of $\beta$-xylosidase pH 6.0 and $40^{\circ}C$ , and that of $\alpha$-arabinofuranosidase pH 5.0 and $50^{\circ}C$. respectively. a-Glucosidase was stable at pH 4.0-9.0. Jj-glucosidase at pH 4.0-7.0. $\beta$-galactosidase at pH 4.0-9.0, $\beta$-xylosidase at pH 4.0-6.0, and /3-arabinofuranosidase at pH 7.0-9.0, respectively.

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