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Asian-Australas J Anim Sci > Accepted Articles
DOI: https://doi.org/10.5713/ajas.18.0455    [Accepted] Published online August 24, 2018.
Isolation and identification of angiotensin I-converting enzyme inhibitory peptides derived from thermolysin-injected beef M. longissimus
Juhui Choe1, Kuk-Hwan Seol2, Hyun-Jin Kim3, Jin-Taek Hwang4, Mooha Lee1, Cheorun Jo1,5,* 
1Seoul National University, Seoul, Korea
2National Institute of Animal Science, Rural Development Administration, Wanju, Korea
3Department of Food Science and Technology, Gyeongsang National Unviersity, Jinju, Korea
4Korea Food Research Institute, Wanju, Korea
5Institute of Green Bio Sciecne and Technology, Seoul National University, Pyeongchang, Korea
Correspondence:  Cheorun Jo, Tel: 02-880-4804, Fax: 02-873-2271, Email: cheorun@snu.ac.kr
Received: 15 June 2018   • Revised: 16 August 2018   • Accepted: 23 August 2018
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.


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.
Keywords: Beef; Injection; Thermolysin; ACE inhibitory activity; Bioactive peptides

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