Purification and Properties of Bacillus coagulans Cyclomaltodextrin Glucanotransferase

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概要

• 論文の詳細を見る

• Cyclomaltodextrin glucanotransferase(CGTase), produced in a culture filtrate by Bacillus coagulans, was purified to a single, homogeneous protein. It has a monomeric structure with a molecular weight of 65,000,isoelectric point of 4.6,and contains 2mol of Ca^<2+> per mol of the enzyme. The enzyme was most active at pH6.0 and at 70℃. It did nol lose its activity by heat treatment at 70℃ for 10min in the presence of CaCl_2 in the pH range of 5.5〜9.5,and by incubation in the pH range of 5.0〜10.5 at 4℃ for one month. The enzyme converted about 60% of potato starch to cyclodextrins for 20h at 50℃, and the ratio of α- : β- : γ-cyclodextrin produced was 8.1 : 8.9 : 1.0. B. coagulans CGTase was compared with B. macerans CGTase which was purified by the same method.

• 社団法人日本生物工学会の論文
• 1991-05-25

著者

• YAGI Toshiharu

  Department of Bioresources Science, Faculty of Agriculture, Kochi University

• Yagi T

  Kochi Univ. Kochi Jpn

• Yagi Toshiharu

  Department Of Agricultural Chemistry Kochi University

• YAMAMOTO Shinpei

  Department of Bioresources Science, Faculty of Agriculture, Kochi University

• Yamamoto Shinpei

  Department Of Agricultural Chemistry Faculty Of Agriculture Kochi University

• Yamamoto Shinpei

  Department Of Agricultural Chemistry Kochi University

• Yamamoto Shinpei

  Department Of Bioresources Science Kochi University

• AKIMARU Kunihiro

  Department of Environmental and Occupational Health, Kochi Medical School

• Akimaru Kunihiro

  Env Occup Health, Kochi Med Sch

• Akimaru K

  Env Occup Health Kochi Med Sch

• Akimaru Kunihiro

  Department Of Environmental And Occupational Health Kochi Medical School

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