Teagasc, The Irish Agricultural and Food Development Authority, Food BioSciences Department, Ashtown, Dublin 15, Dublin, Ireland.
Teagasc, The Irish Agricultural and Food Development Authority, Food BioSciences Department, Moorepark, Fermoy, Co. Cork, Ireland.
J Agric Food Chem. 2015 Oct 7;63(39):8676-84. doi: 10.1021/acs.jafc.5b03167. Epub 2015 Sep 28.
Bovine fibrinogen is currently used in the food industry as a binding agent in restructured meat products. However, this protein is underused as a source of bioactive peptides. In this study, a number of novel angiotensin-I-converting enzyme (ACE-I) and renin inhibitory peptides were identified and enriched from a bovine fibrinogen fraction. Fibrinogen was isolated and enriched from bovine blood and hydrolyzed with the food-grade enzyme papain, which was selected for use using in silico analysis. The generated hydrolysate was subjected to ultrafiltration and its peptide profile characterized by liquid chromatography-tandem mass spectrometry. A number of peptides were identified and chemically synthesized to confirm their bioactivity in vitro. Identified peptides included the multifunctional tripeptide SLR, corresponding to f(35-37) of the β-chain of bovine fibrinogen with ACE-I and renin IC50 values of 0.17 and 7.2 mM, respectively. Moreover, the resistance of identified peptides to gastrointestinal degradation and their bitterness were predicted using in silico methods.
牛纤维蛋白原目前在食品工业中用作重组肉产品的黏合剂。然而，这种蛋白质作为生物活性肽的来源未得到充分利用。在这项研究中，从牛纤维蛋白原部分中鉴定和富集了一些新型血管紧张素转化酶（ACE-I）和肾素抑制肽。纤维蛋白原从牛血中分离和富集，并用食品级酶木瓜蛋白酶水解，使用计算机分析选择用于使用。所得水解产物进行超滤，并通过液相色谱-串联质谱法对其肽谱进行表征。鉴定出了一些肽，并通过化学合成来确认它们在体外的生物活性。鉴定出的肽包括多功能三肽 SLR，对应于牛纤维蛋白原β链的 f(35-37)，其 ACE-I 和肾素 IC50 值分别为 0.17 和 7.2mM。此外，还使用计算机方法预测了鉴定出的肽对胃肠道降解的抗性及其苦味。
