Characterization of Angiotensin I-Converting Enzyme (ACE) inhibitory peptides produced in fermented camel milk (Indian breed) by Lactobacillus acidophilus NCDC-15

2022 ◽  
Author(s):  
Divyang Solanki ◽  
Amar Sakure ◽  
Sangeeta Prakash ◽  
Subrota Hati
Keyword(s):  
Lactobacillus Acidophilus ◽  
Camel Milk ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human αs1-casein expressed in Escherichia coli

1999 ◽  
Vol 66 (3) ◽  
pp. 431-439 ◽  
Author(s):  
YOO-KYEONG KIM ◽  
SUN YOON ◽  
DAE-YEUL YU ◽  
BO LÖNNERDAL ◽  
BONG-HYUN CHUNG
Keyword(s):  
Escherichia Coli ◽  
Amino Acid Sequences ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Treatment Of Hypertension ◽  
Ace Inhibitory

Recombinant human αs1-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.

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