Purification and Properties of Trehalose-Synthesizing Enzyme from Pseudomonas sp. F1

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概要

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• The trehalose-synthesizing enzyme, which catalyzes the conversion of maltose to trehalose by intramolecullar transglucosylation, was purified from a bacterium, Pseudomonas sp. F1. Its molecular mass was estimated to be 250 kDa by gel filtration and 67 kDa by SDS-polyacrylamide gel electrophoresis, and its pI was 5.8. The native enzyme may consist of 4 subunits. The enzyme was active on maltose and trehalose among saccharides tested as substrates. The N-terminal amino acid of the enzyme was threonine.

• 社団法人日本生物工学会の論文
• 1997-10-25

著者

• Yamagishi Masaaki

  Numazu Industrial Research Institute Of Shizuoka Prefecture

• Ono T

  Shigei Medical Research Inst. Okayama

• YOSHINAGA Koichi

  Faculty of Science, Shizuoka University

• Ohta T

  Numazu Industrial Res. Inst. Shizuoka Prefecture Numazu‐shi Jpn

• Wada T

  Fuji Nihon Seito Corp. Shizuoka Jpn

• OHGUCHI MASAO

  Fuji Seito Co. Ltd.

• KUBOTA NORIO

  Fuji Seito Co. Ltd.

• WADA TADASHI

  Fui Seito Co. Ltd.

• URITANI MASAHIRO

  Faculty of Science, Shizuoka University

• YAGISAWA MASAKO

  Faculty of Science, Shizuoka University

• OHISHI KAZUO

  Numazu Industrial Research Institute of Shizuoka Prefecture

• OHTA TOSHIYA

  Numazu Industrial Research Institute of Shizuoka Prefecture

• ISHIKAWA KATSUTOSHI

  Faculty of Science, Shizuoka University

• Ohguchi M

  Fuji Nihon Seito Corp. Shizuoka Jpn

• Ohguchi Masao

  Fuji Nihon Seito Corporation

• Ohishi K

  United Graduate School Of Agricultural Sciences Gifu University

• Yamagishi M

  Tachikawa Hospital Tachikawa Jpn

• Ishikawa Katsutoshi

  Faculty Of Science Shizuoka University

• Uritani Masahiro

  Faculty Of Science Shizuoka University

• Yoshinaga Koichi

  Faculty Of Science Shizuoka University

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