Isolation from α-Zein of Thermolysin Peptides with Angiotensin I-Converting Enzyme Inhibitory Activity

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概要

• 論文の詳細を見る

• Urea-denatured α-zein was almost completely hydrolyzed into small peptides by digestion with 1/100 (w/w) of thermolysin at 37℃ for 3h. The angiotenisin I-converting enzyme (ACE) inhibitory activity (IC_<50> of the thermolysin digest of total α-zein was 24.5μg/ml, and most of the peptide fractions from Z19 α-zein and total α-zein separated by reverse-phase HPLC had more or less ACE inhibitory activity. From these fractions, thirty-six peptides, including 5 dipeptides, 14 tripeptides, 9 tetrapeptides, 5 pentapeptides, and 3 hexapeptides, were purified and their amino acid sequences were determined.

• 社団法人日本農芸化学会の論文
• 1996-04-23

著者

• Funatsu Gunki

  Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric

• Suzuki Kazumasa

  San-ei Sucrochemical Co. Ltd.

• YANO Seiko

  Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University

• Yano Seiko

  Laboratory Of Protein Chemistry And Engineering Faculty Of Agriculture Kyushu University

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