Antioxidant capacity and identification of radical scavenging peptides from Crema de Chiapas, Fresco and Cocido cheeses.

Bioactive peptides may positively impact bodily functions. One of these are the antioxidant peptides which are well documented for a wide variety of food matrices, mostly from plant sources. Nevertheless, information of antioxidant milk-derived peptides is still a little-known field. The present study was aimed to evaluating the antioxidant capacity (AC) in vitro of water soluble extracts < 3 kDa (WSE) from three artisanal Mexican cheeses: Crema de Chiapas (CrC), Fresco (FC) and Cocido (CC). This study was carried out for cheeses of different days of storage (0, 5, 10, 15, and 20) at 4 °C. AC was assayed to the respective WSE by 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) diamoniun salt (ABTS) and oxygen radical absorbance capacity (ORAC) methods and those WSE that showed the most antioxidant capacity from each cheese were analyzed by using RP-HPLC/MS to identify and characterize the novel specific peptides. All the WSE analyzed show antioxidant capacity, especially those from CrC and CC which display the highest AC at 15 days of storage. Regarding to WSE from FC, the AC was constant during storage. Identified structures reveal that these novel peptides possess high content of specific amino acids, mainly proline, valine, leucine and phenylalanine, of which it has already been shown antioxidant properties. This study demonstrate that these artisanal Mexican cheeses are sources of potential antioxidant peptides.

Invited review: Fermented milk as antihypertensive functional food.

Over the past decade, interest has risen in fermented dairy foods that promote health and could prevent diseases such as hypertension. This biological effect has mainly been attributed to bioactive peptides encrypted within dairy proteins that can be released during fermentation with specific lactic acid bacteria or during gastrointestinal digestion. The most studied bioactive peptides derived from dairy proteins are antihypertensive peptides; however, a need exists to review the different studies dealing with the evaluation of antihypertensive fermented milk before a health claim may be associated with the product. Thus, the objective of this overview was to present available information related to the evaluation of fermented milk containing antihypertensive peptides by in vitro and in vivo studies, which are required before a fermented functional dairy product may be introduced to the market. Although commercial fermented milks with antihypertensive effects exist, these are scarce and most are based on Lactobacillus helveticus. Thus, a great opportunity is available for the development of functional dairy products with new lactic acid bacteria that support heart health through blood pressure- and heart rate-lowering effects. Hence, the consumer may be willing to pay a premium for foods with important functional benefits.

Novel angiotensin I-converting enzyme inhibitory peptides produced in fermented milk by specific wild Lactococcus lactis strains.

The ability of specific wild Lactococcus lactis strains to hydrolyze milk proteins to release angiotensin I-converting enzyme (ACE) inhibitory peptides was evaluated. The peptide profiles were obtained from the <3 kDa water-soluble extract and subsequently fractionated by reversed-phase HPLC. The fractions with the lowest half-maximal inhibitory concentration estimated values (peptide concentration necessary to inhibit ACE activity by 50%) were Lc. lactis NRRL B-50571 fraction (F)1 (0.034 ± 0.002 µg/mL; mean ± SD) and Lc. lactis NRRL B-50572B F 0005 (0.041 ± 0.003 µg/mL; mean ± SD). All peptide fractions were analyzed by reversed-phase HPLC tandem mass spectrometry. Twenty-one novel peptide sequences associated with ACE inhibitory (ACEI) activity were identified. Several novel ACEI peptides presented peptides encrypted with proven hypotensive activity. In conclusion, specific wild Lc. lactis strains were able to hydrolyze milk proteins to generate potent ACEI peptides. However, further studies are necessary to find out the relationship between Lc. lactis strain proteolytic systems and their ability to biogenerate hypotensive peptides.

Angiotensin-converting enzyme inhibitory activity in Mexican Fresco cheese.

The objective of this study was to evaluate if Mexican Fresco cheese manufactured with specific lactic acid bacteria (LAB) presented angiotensin I-converting enzyme inhibitory (ACEI) activity. Water-soluble extracts (3 kDa) obtained from Mexican Fresco cheese prepared with specific LAB (Lactococcus, Lactobacillus, Enterococcus, and mixtures: Lactococcus-Lactobacillus and Lactococcus-Enterococcus) were evaluated for ACEI activity. Specific peptide fractions with high ACEI were analyzed using reverse phase-HPLC coupled to mass spectrometry for determination of amino acid sequence. Cheese containing Enterococcus faecium or a Lactococcus lactis ssp. lactis-Enterococcus faecium mixture showed the largest number of fractions with ACEI activity and the lowest half-maximal inhibitory concentration (IC(50); <10 µg/mL). Various ACEI peptides derived from ß-casein [(f(193-205), f(193-207), and f(193-209)] and α(S1)-casein [f(1-15), f(1-22), f(14-23), and f(24-34)] were found. The Mexican Fresco cheese manufactured with specific LAB strains produced peptides with potential antihypertensive activity.