Novel agiotensin-I-converting enzyme inhibitory peptides derived from recombinant human alphas1-casein expressed in Escherichia coli

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Title
Novel agiotensin-I-converting enzyme inhibitory peptides derived from recombinant human alphas1-casein expressed in Escherichia coli
Author(s)
Yoo Kyeong Kim; Sun Yoon; Dae Yeul Yu; Bo Lonnerdal; Bong Hyun Chung
Bibliographic Citation
Journal of Dairy Research, vol. 66, pp. 431-439
Publication Year
1999
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.
Keyword
peptide fragmentsrecombinant proteins
ISSN
0022-0299
Publisher
Cambridge Univ Press
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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