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

  • Choe, Juhui (Department of Agricultural Biotechnology, Center for Food and Bioconvergence, and Research Institute of Agriculture and Life Science, Seoul National University) ;
  • Seol, Kuk-Hwan (National Institute of Animal Science, Rural Development Administration) ;
  • Kim, Hyun-Jin (Department of Food Science and Technology, Gyeongsang National University) ;
  • Hwang, Jin-Taek (Korea Food Research Institute) ;
  • Lee, Mooha (Department of Agricultural Biotechnology, Center for Food and Bioconvergence, and Research Institute of Agriculture and Life Science, Seoul National University) ;
  • Jo, Cheorun (Department of Agricultural Biotechnology, Center for Food and Bioconvergence, and Research Institute of Agriculture and Life Science, Seoul National University)
  • Received : 2018.06.15
  • Accepted : 2018.08.23
  • Published : 2019.03.01

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 $5^{\circ}C$. 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 ($IC_{50}$) of each peptide was evaluated. Results: The Leu-Ser-Trp, Phe-Gly-Tyr, and Tyr-Arg-Gln peptides exhibited the strongest ACE inhibitory activity ($IC_{50}$ 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

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