| Autor: |
Begunova AV; Federal State Budgetary Scientific Institution 'All-Russian Research Institute of Dairy Industry', 115093 Moscow, Russia., Savinova OS; A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia., Glazunova OA; A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia., Moiseenko KV; A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia., Rozhkova IV; Federal State Budgetary Scientific Institution 'All-Russian Research Institute of Dairy Industry', 115093 Moscow, Russia., Fedorova TV; A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia. |
| Abstrakt: |
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 Lactobacillus spp. Here we present the study of milk fermentation by Lactobacillus helveticus NK1, Lactobacillus rhamnosus F and Lactobacillus reuteri 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 L. helveticus NK1 was two times higher than that of L. rhamnosus 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 L. rhamnosus F. In addition, it was demonstrated that these potential ACE-inhibiting peptides originated from the C-terminus of α S2 -casein. |
