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

Asian-Australasian Journal of Animal Sciences

Cheorun Jo¹  Mooha Lee¹  Juhui Choe¹  Hyun-Jin Kim²  Jin-Taek Hwang³  Kuk-Hwan Seol⁴ 

[1] Department of Agricultural Biotechnology, Center for Food and Bioconvergence, and Research Institute of Agriculture and Life Science, Seoul National University, Seoul 08826, Korea;Department of Food Science and Technology, Gyeongsang National University, Jinju 52828, Korea;Korea Food Research Institute, Wanju 55365, Korea;National Institute of Animal Science, Rural Development Administration, Wanju 55365, Korea;

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

DOI  :  10.5713/ajas.18.0455

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown