Purification and Properties of γ-Glutamyltranspeptidase from Bacillus subtilis (natto)(Biological Chemistry)
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概要
- 論文の詳細を見る
To understand the mechanism by which γ-polyglutamic acid (γ-PGA) in the sticky material of natto was synthesized, we purified the γ-glutamyltranspeptidase (γ-GTP)(EC2.3.2.2) from the culture broth of Bacillus subtilis (natto) to homogeneity. γ-GTP was composed of two subunits with molecular weight of 45,000 and 22,000. The N-terminal amino acid sequence of light subunit was homologous with that of γ-GTP from Escherichia coli. The optimum pH and temperature of activity were 8.5 and 60℃. The enzyme was inactivated by incubation for 15min at pH 8.0 and 55℃, but little loss of the activity was detected at 40℃. γ-GTP used glutamine as a γ-glutamyl donor and acceptor for γ-PGA synthesis. Dipeptides were better γ-glutamyl acceptors than free amino acids.
- 社団法人日本農芸化学会の論文
- 1991-12-23
著者
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OGAWA Yoshihiro
Research and Development Division, Kikkoman Corporation
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MOTAI Hiroshi
Research and Development Division, Kikkoman Corporation
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Ogawa Yoshihiro
Research And Development Division Kikkoman Corporation
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Motai Hiroshi
Research And Development Division Kikkoman Corporation
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Hamano Mitsutoshi
Research and Development Division, Kikkoman Corporation
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Hosoyama Hiroshi
Research And Development Division Kikkoman Corporation
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Hamano Mitsutoshi
Research And Development Division Kikkoman Corporation
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