Isolation and identification of angiotensin I-converting enzyme inhibitory peptides derived from thermolysin-injected beef M. longissimus

Asian-Australasian Journal of Animal Sciences
Juhui ChoeCheorun Jo

Abstract

This study identified angiotensin I-converting enzyme (ACE) inhibitory peptides in beef M. longissimus injected with thermolysin (80 ppm) and stored for 3 days at 5°C. Crude peptides (molecular weight <3 kDa) were obtained from the thermolysin hydrolysate and separated into seven fractions. Fraction V showing the highest ACE inhibitory activity was further fractionated, yielding subfractions V-15, V-m1, and V-m2, and selected for superior ACE inhibitory activity. Finally, twelve peptides were identified from the three peak fractions and the ACE inhibitory activity (IC50) of each peptide was evaluated. The Leu-Ser-Trp, Phe-Gly-Tyr, and Tyr-Arg-Gln peptides exhibited the strongest ACE inhibitory activity (IC50 values of 0.89, 2.69, and 3.09 mM, respectively) and had higher concentrations (6.63, 10.60, and 29.91 pg/g; p<0.05) relative to the other peptides tested. These results suggest that the thermolysin injection process is beneficial to the generation of bioactive peptides with strong ACE inhibitory activity.

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Citations

Nov 28, 2018·Korean Journal for Food Science of Animal Resources·Bumjin ParkCheorun Jo
Mar 19, 2019·Food Science of Animal Resources·Kyung Chul KohJuhui Choe
Jun 20, 2019·Protein and Peptide Letters·Sulochana Priya
Oct 3, 2019·Food & Function·Julia BechauxVéronique Sante-Lhoutellier
Aug 25, 2019·Antioxidants·Bartosz KulczyńskiAnna Gramza-Michałowska
Dec 20, 2020·Food Chemistry·Arshdeep KaurSawinder Kaur
Apr 26, 2020·Food Research International·Julia BechauxVéronique Santé-Lhoutellier
Jul 25, 2021·International Journal of Environmental Research and Public Health·Irina ChernukhaDaniil Khvostov

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Methods Mentioned

BETA
gel filtration

Software Mentioned

SAS
MassLynx

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