Begunova Anna V, Savinova Olga S, Glazunova Olga A, Moiseenko Konstantin V, Rozhkova Irina V, Fedorova Tatyana V
Federal State Budgetary Scientific Institution "All-Russian Research Institute of Dairy Industry", 115093 Moscow, Russia.
A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia.
Foods. 2020 Dec 23;10(1):17. doi: 10.3390/foods10010017.
Bioactive peptides derived from milk proteins are an active research area. Exhibiting numerous positive physiological effects on digestive, cardiovascular, immune and nervous systems, these peptides thought to be one of the most promising ingredients for functional food. Generally, these peptides are inactive within the parent proteins and can be liberated during milk fermentation by the specific proteolytic systems of various spp. Here we present the study of milk fermentation by NK1, F and LR1 strains. It was demonstrated that the antioxidant activity of the milk fermented by these strains concomitantly increased with the strains' proteolytic activity. For the angiotensin I-converting enzyme (ACE) inhibitory activity, the same tendency was not observed. Although the proteolytic activity of NK1 was two times higher than that of F, the milk fermented by these strains showed comparable ACE inhibition. The analysis of the peptide profiles of the fermented milk samples allowed us to hypothesize that some previously unreported peptides can be produced by F. In addition, it was demonstrated that these potential ACE-inhibiting peptides originated from the C-terminus of α-casein.
源自乳蛋白的生物活性肽是一个活跃的研究领域。这些肽对消化、心血管、免疫和神经系统具有多种积极的生理作用，被认为是功能性食品最具前景的成分之一。一般来说，这些肽在母体蛋白质中是无活性的，可在牛奶发酵过程中被各种菌株的特定蛋白水解系统释放出来。在此，我们展示了NK1、F和LR1菌株对牛奶发酵的研究。结果表明，这些菌株发酵的牛奶的抗氧化活性随菌株的蛋白水解活性而同步增加。对于血管紧张素I转换酶（ACE）抑制活性，未观察到相同趋势。尽管NK1的蛋白水解活性比F高两倍，但这些菌株发酵的牛奶显示出相当的ACE抑制作用。对发酵乳样品的肽谱分析使我们推测F可能产生一些以前未报道的肽。此外，还证明这些潜在的ACE抑制肽源自α-酪蛋白的C末端。
