Abstract
Recombinant human α(s1)-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II. B-II and C, were isolated and their amino acid sequences identified as Tyr-Pro-Glu-Arg (residues 8-11), Tyr-Tyr-Pro-Gln-Ile-Met-Gln-Tyr (residues 136-143) and Asn-Asn-Val-Met-Leu-Gln-Trp (residues 164-170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132.5, 24.8 and 41.0 μmol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 431-439 |
| Number of pages | 9 |
| Journal | Journal of Dairy Research |
| Volume | 66 |
| Issue number | 3 |
| DOIs | |
| State | Published - Aug 1999 |
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ASJC Scopus subject areas
- Animal Science and Zoology
- Applied Microbiology and Biotechnology
- Food Science
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Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human α(s1)-casein expressed in Escherichia coli. / Kim, Yoo Kyeong; Yoon, Sun; Yu, Dae Yeul; Lönnerdal, Bo; Chung, Bong Hyun.
In: Journal of Dairy Research, Vol. 66, No. 3, 08.1999, p. 431-439.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human α(s1)-casein expressed in Escherichia coli
AU - Kim, Yoo Kyeong
AU - Yoon, Sun
AU - Yu, Dae Yeul
AU - Lönnerdal, Bo
AU - Chung, Bong Hyun
PY - 1999/8
Y1 - 1999/8
N2 - Recombinant human α(s1)-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II. B-II and C, were isolated and their amino acid sequences identified as Tyr-Pro-Glu-Arg (residues 8-11), Tyr-Tyr-Pro-Gln-Ile-Met-Gln-Tyr (residues 136-143) and Asn-Asn-Val-Met-Leu-Gln-Trp (residues 164-170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132.5, 24.8 and 41.0 μmol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.
AB - Recombinant human α(s1)-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II. B-II and C, were isolated and their amino acid sequences identified as Tyr-Pro-Glu-Arg (residues 8-11), Tyr-Tyr-Pro-Gln-Ile-Met-Gln-Tyr (residues 136-143) and Asn-Asn-Val-Met-Leu-Gln-Trp (residues 164-170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132.5, 24.8 and 41.0 μmol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.
UR - http://www.scopus.com/inward/record.url?scp=0033178683&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033178683&partnerID=8YFLogxK
U2 - 10.1017/S0022029999003556
DO - 10.1017/S0022029999003556
M3 - Article
C2 - 10480081
AN - SCOPUS:0033178683
VL - 66
SP - 431
EP - 439
JO - Journal of Dairy Research
JF - Journal of Dairy Research
SN - 0022-0299
IS - 3
ER -