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Isolation of Amylolytic Bifidobacterium sp. Int-57 and Characterization of Amylase
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  • Isolation of Amylolytic Bifidobacterium sp. Int-57 and Characterization of Amylase
  • Isolation of Amylolytic Bifidobacterium sp. Int-57 and Characterization of Amylase
저자명
Ji. Geun-Eog,Han. Hee-Kyung,Yun. Seong-Wook
간행물명
Journal of microbiology and biotechnology
권/호정보
1992년|2권 2호|pp.85-91 (7 pages)
발행정보
한국미생물생명공학회
파일정보
정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

The intestinal microflora of humans is an extraordinarily complex mixture of microorganisms, the majority of which are anaerobic microorganisms. The distribution of amylolytic microorganisms in the human large intestinal tract was investigated in various individuals of differing ages using anaerobic culture techniques. A large percentage of the amylolytic microorganisms present belonged to the Genus Bifidobacteria. The number of Bifidobacteria increased significantly at two years of age. Adults and children above 2 years old carried about $0.8{ imes}10^9-2.0{ imes}10^{10}$ colony forming units (CFU/gram) of amylolytic Bifidobacteria. Among these amylolytic Bifidobacteria, Int-57 was chosen for further studies. Between 65% and 85% of the amylase produced was secreted and the remaining amylase was bound to the cell wall facing the outside. Amylase production could be induced by starch in a stable form. When cells were grown on maltose or glucose, amylase production was much lower than on starch and amylase activity disappeared after 24 hours growth on these media. Partially purified enzymes showed optimum activity at a temperature of $50^{circ}C$ and at an optimum pH of 5.5, respectively. Heat treatment at $70^{circ}C$ for 30 minutes almost completely inactivated amylase. The hydrolysis products of starch were mainly maltose and maltotriose. Soluble starch, amylose, amylopectin, and $gamma$-cyclodextrin($gamma$-CD) were easily hydrolyzed. The rate of hydrolysis of $alpha$-CD and $eta$-CD was slower than that of $gamma$-CD. Carboxymethyl cellulose, $eta$-1, 3-glucan and inulin were not hydrolyzed.