Isolation and identification of angiotensin I-converting enzyme inhibitory peptides derived from thermolysin-injected beef M. longissimusopen access
- Choe, Juhui; Seol, Kuk-Hwan; Kim, Hyun-Jin; Hwang, Jin-Taek; Lee, Mooha; Jo, Cheorun
- Issue Date
- ASIAN-AUSTRALASIAN ASSOC ANIMAL PRODUCTION SOC
- Beef; Injection; Thermolysin; Angiotensin I-converting Enzyme (ACE) Inhibitory Activity; Bioactive Peptides
- ASIAN-AUSTRALASIAN JOURNAL OF ANIMAL SCIENCES, v.32, no.3, pp.430 - 436
- Journal Title
- ASIAN-AUSTRALASIAN JOURNAL OF ANIMAL SCIENCES
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- End Page
- 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 degrees 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.
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