Choe Juhui, Seol Kuk-Hwan, Kim Hyun-Jin, Hwang Jin-Taek, Lee Mooha, Jo Cheorun
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.
Asian-Australas J Anim Sci. 2019 Mar;32(3):430-436. doi: 10.5713/ajas.18.0455. Epub 2018 Aug 24.
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.
本研究鉴定了经嗜热菌蛋白酶(80 ppm)注射并在5°C下储存3天的牛肉背最长肌中的血管紧张素I转换酶(ACE)抑制肽。
从嗜热菌蛋白酶水解物中获得粗肽(分子量<3 kDa),并分离成七个组分。对显示出最高ACE抑制活性的组分V进一步分级分离,得到亚组分V-15、V-m1和V-m2,并因其优异的ACE抑制活性而被选中。最后,从三个峰组分中鉴定出12种肽,并评估了每种肽的ACE抑制活性(IC50)。
Leu-Ser-Trp、Phe-Gly-Tyr和Tyr-Arg-Gln肽表现出最强的ACE抑制活性(IC50值分别为0.89、2.69和3.09 mM),并且相对于其他测试肽具有更高的浓度(6.63、10.60和29.91 pg/g;p<0.05)。
这些结果表明,嗜热菌蛋白酶注射过程有利于生成具有强ACE抑制活性的生物活性肽。