清酒麹酸性カルボキシペプチダーゼの精製と諸性質 : 清酒醸造におけるアミノ酸の生成(第3報)

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Aspergillus oryzae acid carboxypeptidase (peptidyl-L-amino-acid hydrolase, EC 3.4.16.1) Ia, Ib, IIa, and IIb were isolated and purified from sake koji extract by ethanol precipitation, batchwise treatment with DEAE-Sephadex A-50,DEAE-cellulose ion-exchange chromatography, column chromatography with ω-amino dodecyl agarose, and Sepacryl S-300 or Sephacryl S-200 gel chromatography.By gel chromatography, the molecular weight was estimated to be about 230,000 for acid carboxypeptidase Ia, 133,000 for Ib, and 59,000 for IIa and IIb. The isoelectric points of acid carboxypeptidases Ia, Ib, IIa, and IIb were 4.60,4.52,4.20,and 4.11,respectively.The optimal pH and temperature for the activity of each of these acid carboxypeptidases were 3.0 and 45℃, respectively. Of the metal ions tested, Cu^+ was the most potent inhibitor of enzyme activity. Each enzyme was inhibited by diisopropyl fluorophosphate, monoiodoacetate, p-chloromercuribenzoate, N-ethylmaleimide, and sodium dodecylsulfate.The hydrolytic action of each enzyme on 31 kinds of N-acyl-peptides and amides was examined. When L-Ala and L-His were present at the penultimate position of the carboxyterminus of the peptide, acid carboxypeptidase Ia and Ib hydrolyzed the carboxyterminal peptide bond much more rapidly than the other enzymes.Every enzyme hydrolyzed bradykinin and angiotensin I sequentially from each carboxyterminus. When L-Pro was the penultimate amino acid, the carboxyterminal amino acid newly formed was most readily released by acid carboxypeptidase Ia and least readily by acid carboxypeptidase IIa and IIb.
社団法人日本生物工学会の論文
1987-01-25

清酒麹酸性カルボキシペプチダーゼの精製と諸性質 : 清酒醸造におけるアミノ酸の生成(第3報)

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