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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.

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



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.


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

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