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Asian-Australas J Anim Sci. 2019 Mar;32(3):430-436. doi: 10.5713/ajas.18.0455. Epub 2018 Aug 24.

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

Author information

1
Department of Agricultural Biotechnology, Center for Food and Bioconvergence, and Research Institute of Agriculture and Life Science, Seoul National University, Seoul 08826, Korea.
2
National Institute of Animal Science, Rural Development Administration, Wanju 55365, Korea.
3
Department of Food Science and Technology, Gyeongsang National University, Jinju 52828, Korea.
4
Korea Food Research Institute, Wanju 55365, Korea.
5
Institute of Green Bio Science and Technology, Seoul National University, Pyeongchang 25354, Korea.

Abstract

OBJECTIVE:

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.

METHODS:

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.

RESULTS:

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.

CONCLUSION:

These results suggest that the thermolysin injection process is beneficial to the generation of bioactive peptides with strong ACE inhibitory activity.

KEYWORDS:

Angiotensin I-converting Enzyme (ACE) Inhibitory Activity; Beef; Bioactive Peptides; Injection; Thermolysin

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