Bioactive protein hydrolysates obtained from amaranth by fermentation with lactic acid bacteria and Bacillus species.

Protein hydrolysates are a promising source of bioactive peptides. One strategy by which they can be obtained is fermentation. This method uses the proteolytic system of microorganisms to hydrolyze the parental protein. Fermentation is a little-explored method for obtaining protein hydrolysates from amaranth. Different strains of lactic acid bacteria (LAB) and Bacillus species isolated from goat milk, broccoli, aguamiel, and amaranth flour were used in this work. First, the total protein degradation (%TPD) of amaranth demonstrated by the strains was determined. The results ranged from 0 to 95.95%, the strains that produced a higher %TPD were selected. These strains were identified by molecular biology and were found to correspond to the genera Enterococcus, Lactobacillus, Bacillus, and Leuconostoc. Fermentation was carried out with amaranth flour and the selected strains. After this process, water/salt extracts (WSE) containing the released protein hydrolysates were obtained from amaranth doughs. The peptide concentration was measured by the OPA method. The antioxidant, antihypertensive and antimicrobial activity of the WSE was evaluated. In the FRAP test, the best WSE was LR9 with a concentration of 1.99 µMTE/L ± 0.07. In ABTS, 18C6 obtained the highest concentration with 19.18 µMTE/L ± 0.96. In the DPPH test, there was no significant difference. In terms of antihypertensive activity, inhibition percentages ranging from 0 to 80.65% were obtained. Some WSE were found to have antimicrobial properties against Salmonella enterica and Listeria monocytogenes. Fermentation of amaranth with LAB and Bacillus spp. allowed the release of protein hydrolysates with antioxidant, antihypertensive, and antimicrobial activity.

Enzymatic hydrolysis and microbial fermentation: The most favorable biotechnological methods for the release of bioactive peptides.

Bioactive peptides are biomolecules derived from proteins. They contain anywhere from 2 to 20 amino acids and have different bioactivities. For example, they have antihypertensive activity, antioxidant activity, antimicrobial activity, etc. However, bioactive peptides are encrypted and inactive in the parental protein, so it is necessary to release them to show their bioactivity. For this, there are different methods, where biotechnological methods are highly favorable, highlighting enzymatic hydrolysis and microbial fermentation. The choice of the method to be used depends on different factors, which is why it is essential to know about the process, its principle, and its advantages and disadvantages. The process of peptide release is critical to generate various peptide sequences, which will produce different biological effects in the hydrolysate. This review focuses on providing extensive information on the enzymatic method and microbial fermentation to facilitate selecting the method that provides the most benefits.