Bifidobacterium breveの生産するプロリンイミノペプチダーゼの精製とその性質について

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タイトル別名
  • Purification and Some Properties of a Praline Iminopeptidase from Bifidobacterium breve
  • Bifidobacterium breve ノ セイサンスル プロリンイミノペ

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抄録

A proline iminopeptidase (EC 3.4.11.5) was purified about 3, 400-fold (specific activity 590 units/mg protein) with a yield of 5.1% from the cell-free extract of Bifidobacterium breve (MT-17) by a procedure including protamine sulfate fractionation, ammonium sulfate fractionation, DEAE-Sepharose CL-6B chromatography, hydroxylapatite chromatography, rechromatography on DEAE-Sepharose CL-6B, Chromatofocusing, and Polyacrylamide disc gel electrophoresis. The main results obtained were as follows: 1. The purified enzyme showed a single protein band on polyacrylamide disc gel electrophoresis at pH 6.6, and an isoelectric point pI 3.60 on chromatofocusing. 2. The molecular weight of the enzyme was estimated to be about 67, 000 by gel filtration on Sephadex G-75 and about 67, 500 by sodium dodecyl sulfate gel electrophoresis, respectively. 3. The enzyme exhibited a pH optimum at 6.8, temperature optimum at 37°C and was stable up to 40°C for 30min in heating. 4. The enzyme was not activated by metal ions, and was unaffected by EDTA and 1, 10-phenanthroline. It was sensitive towards monoiodoacetic acid, p-chloromercuribenzoate, N-ethylmaleimide, phenylmethylsulfonyl fluoride, and benzamidine. 5. The enzyme hydrolyzed many peptides with N-terminal L-proline residues and also acted on hydroxyproline-β-naphthylamide. The relative rate of hydrolysis of hydroxyproline-β-naphthylamide was approximately two times higher than proline-β-naphthylamide.

収録刊行物

  • 日本畜産学会報

    日本畜産学会報 56 (6), 484-494, 1985

    公益社団法人 日本畜産学会

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