Purification and Some Properties of a New Levanase from Bacillus sp. No. 71

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概要

• 論文の詳細を見る

• A levanase from Bacillus sp. was purified to a homogeneous state. The enzyme had a molecular weight of 135,000 and an isoelectric point of pH 4.7. The enzyme was most active at pH 6.0 and 40℃, stable from pH 6.0 to 10.0 for 20hr of incubation at 4℃ and up to 30℃ for 30 min of incubation at pH 6.0. The enzyme activity was inhibited by Ag^+, Hg^<2+>, Cu^<2+>, Fe^<3+>, Pb^<2+>, and p-chloromercuribenzoic acid. The enzyme hydrolyzed levan and phlein endowise to produce levanheptaose as a main product. The limit of hydrolysis of levan and phlein were 71% and 96%, respectively.

• 社団法人日本農芸化学会の論文
• 1992-04-23

著者

• Murakami Hiromi

  Osaka Municipal Technical Res. Inst.

• MIZUTANI Kenji

  Maruzen Pharmaceutical Co., Ltd

• Mizutani K

  Maruzen Pharmaceuticals Co.

• KURAMOTO Takashi

  Maruzen Kasei Co., Ltd.

• KITAHATA Sumio

  Osaka Municipal Technical Research Institute

• KISO TARO

  Osaka Municipal Technical Research Institute

• Murakami H

  Laboratory Of Cellular Regulation Technology Graduate School Of Genetic Resources Technology Kyushu

• KURAMOTO Takayuki

  Research Institute for Advanced Science and Technology, Osaka Prefecture University

• NAKANO HIROFUMI

  Osaka Municipal Technical Research Institute, and Yashiro Co, Ltd.,

• Kitahata S

  Department Of Bioscience And Biotecnology Shinshu University

• Murakami H

  Osaka Municipal Technical Res. Inst.

• Nakano Hirofumi

  Osaka Municipal Technical Research Institute

• Mizutani Kimihiko

  Division Of Applied Life Science Graduate School Of Agriculture Kyoto University

• Nakano Hirofumi

  Department Of Chemistry Faculty Of Science Osaka University

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