Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle

Hiroshi Matsufuji; Toshiro Matsui; Masatoshi Nakashima; Yutaka Osajima; Eiji Seki; Katsuhiro Osajima

doi:10.1271/bbb.58.2244

Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle

Hiroshi Matsufuji, Toshiro Matsui, Masatoshi Nakashima, Yutaka Osajima, Eiji Seki, Katsuhiro Osajima

Food Science and Biotechnology

Research output: Contribution to journal › Article › peer-review

235 Citations (Scopus)

Abstract

The ACE inhibitory activity of an alkaline protease hydrolyzate from sardine muscle did not change after being treated by gastrointestinal proteases (IC₅₀ = 0.082 mg protein/ml). Eleven new ACE inhibitory peptides, constructed with 2 to 4 amino acid residues, were isolated from the hydrolyzate. The ACE inhibitory activity of each was mostly below 100μM of IC₅₀ value; the maximal inhibitory activity was observed for Lys-Trp (IC₅₀ = 1.63 μm). The isolated peptides inhibited ACE competitively, except for Met-Tyr with non-competitive inhibition. As the result of sequence homology, Arg-Val-Tyr isolated from the hydrolyzate was found in the primary structure of angiotensins I, II, and III, and of des Asp[l]-angiotensin I.

Original language	English
Pages (from-to)	2244-2245
Number of pages	2
Journal	Bioscience, biotechnology, and biochemistry
Volume	58
Issue number	12
DOIs	https://doi.org/10.1271/bbb.58.2244
Publication status	Published - 1994

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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title = "Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle",

abstract = "The ACE inhibitory activity of an alkaline protease hydrolyzate from sardine muscle did not change after being treated by gastrointestinal proteases (IC50 = 0.082 mg protein/ml). Eleven new ACE inhibitory peptides, constructed with 2 to 4 amino acid residues, were isolated from the hydrolyzate. The ACE inhibitory activity of each was mostly below 100μM of IC50 value; the maximal inhibitory activity was observed for Lys-Trp (IC50 = 1.63 μm). The isolated peptides inhibited ACE competitively, except for Met-Tyr with non-competitive inhibition. As the result of sequence homology, Arg-Val-Tyr isolated from the hydrolyzate was found in the primary structure of angiotensins I, II, and III, and of des Asp[l]-angiotensin I.",

author = "Hiroshi Matsufuji and Toshiro Matsui and Masatoshi Nakashima and Yutaka Osajima and Eiji Seki and Katsuhiro Osajima",

note = "Funding Information: Acknowledgment. This work was supported by a Grant-in-Aid for Scientific Research in Priority Areas from the Ministry of Education, Science, and Culture of Japan.",

year = "1994",

doi = "10.1271/bbb.58.2244",

language = "English",

volume = "58",

pages = "2244--2245",

journal = "Bioscience, Biotechnology and Biochemistry",

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T1 - Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle

AU - Matsufuji, Hiroshi

AU - Matsui, Toshiro

AU - Nakashima, Masatoshi

AU - Osajima, Yutaka

AU - Seki, Eiji

AU - Osajima, Katsuhiro

N1 - Funding Information: Acknowledgment. This work was supported by a Grant-in-Aid for Scientific Research in Priority Areas from the Ministry of Education, Science, and Culture of Japan.

PY - 1994

Y1 - 1994

N2 - The ACE inhibitory activity of an alkaline protease hydrolyzate from sardine muscle did not change after being treated by gastrointestinal proteases (IC50 = 0.082 mg protein/ml). Eleven new ACE inhibitory peptides, constructed with 2 to 4 amino acid residues, were isolated from the hydrolyzate. The ACE inhibitory activity of each was mostly below 100μM of IC50 value; the maximal inhibitory activity was observed for Lys-Trp (IC50 = 1.63 μm). The isolated peptides inhibited ACE competitively, except for Met-Tyr with non-competitive inhibition. As the result of sequence homology, Arg-Val-Tyr isolated from the hydrolyzate was found in the primary structure of angiotensins I, II, and III, and of des Asp[l]-angiotensin I.

AB - The ACE inhibitory activity of an alkaline protease hydrolyzate from sardine muscle did not change after being treated by gastrointestinal proteases (IC50 = 0.082 mg protein/ml). Eleven new ACE inhibitory peptides, constructed with 2 to 4 amino acid residues, were isolated from the hydrolyzate. The ACE inhibitory activity of each was mostly below 100μM of IC50 value; the maximal inhibitory activity was observed for Lys-Trp (IC50 = 1.63 μm). The isolated peptides inhibited ACE competitively, except for Met-Tyr with non-competitive inhibition. As the result of sequence homology, Arg-Val-Tyr isolated from the hydrolyzate was found in the primary structure of angiotensins I, II, and III, and of des Asp[l]-angiotensin I.

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SN - 0916-8451

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ER -

Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle

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