The study of the intra-specific phylogenetic structure of Leuconostoc oenos is essential to understand the participation of several strains in malo-lactic fermentation (MLF). RFLP of the PCR-amplified 16S-23S rDNA intergenic spacer region (ISR) was performed in Leuc. oenos and other related species. The RFLP patterns with seven endonucleases were identical for the 37 Leuc. oenos strains, but differed from those obtained for all other species tested. This method could provide an invaluable insight for molecular identification of the wine leuconostocs. The RFLP relationships of members of the genera Leuconostoc and Weissella were highly similar to those previously reported by 16S and 23S rRNA sequencing studies. The 16S-23S rDNA ISR was sequenced in five strains of Leuc. oenos. A single tRNA(Ala) was detected. The ISR sequence seems to be identical in the two rRNA (rrn) operons found in Leuc. oenos and no significant sequence variation was observed between strains that revealed relative differences as previously shown by PFGE. Results from the present study demonstrated that Leuc. oenos is phylogenetically a very homogeneous species (according to DNA-DNA hybridization studies) and sustain that this species is different from the genus Leuconostoc. The extremely conserved ISR of these organisms suggests that Leus. oenos strains currently isolated and characterized must have spread with the transfer of viticulture rather than coming from indigenous populations.

Multifunctional peptides, capable of acting on different body systems through multiple mechanisms of action, offer many advantages over monofunctional peptides, including lower adverse side effects and costs. Erythrina edulis (pajuro) is a legume with a large number of high-quality proteins, of which their potential as a source of antioxidant peptides has been recently reported. In this study, the behavior of these proteins under a sequential enzymatic hydrolysis with digestive and microbial enzymes was investigated by evaluating the multi-functionality of the hydrolyzates. The albumin hydrolyzates obtained after the action of pepsin, pancreatin, and Alcalase showed antioxidant, angiotensin-converting enzyme (ACE), α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory activities. The radical scavenging properties of the hydrolyzate could be responsible for the potent protective effects observed in FeSO₄-induced neuroblastoma cells. The findings support the role of pajuro protein as an ingredient of functional foods or nutraceuticals for health promotion and the prevention of oxidative stress, hypertension, and metabolic alteration-associated chronic diseases.

Erythrina edulis Triana ex Micheli is a protein-enriched legume traditionally used for both dietary and medicinal purposes. In this paper, protein concentrate was obtained from the seed flour. SDS-PAGE analysis revealed a high number and intensity of bands in the range between 10 and 90 kDa. Neutrase®, Flavourzyme®, and Alcalase® were used to hydrolyze the protein concentrate at different times. By SDS-PAGE, the lower resistance of proteins to Alcalase® action was observed, providing hydrolyzates with higher radical scavenging activity. The 120 min-hydrolyzate showed ORAC and TEAC values of 2.51 and 0.91 μmol Trolox equivalents/mg of protein, respectively. A fraction lower than 3 kDa and rich in hydrophobic and aromatic amino acids was demonstrated to be mainly responsible for the observed activity. E. edulis could be a new alternative in the formulation of functional foods not only for its high protein content but also for the potential biological properties of its hydrolyzates.

Lupinus mutabilis (tarwi) is a cultivated legume used principally as a protein source in human and animal nutrition. In this study, protein concentrate was obtained from debittered and defatted tarwi seed flour. SDS-PAGE analysis revealed the presence of highly intense bands ranged between 35 and 60 kDa. Tarwi protein concentrate was subjected to the action of alcalase to produce hydrolyzates with antioxidant activity. A central composite design was employed to study the effect of the experimental variables, enzyme/substrate ratio and incubation time, on the degree of hydrolysis and the radical scavenging capacity. The influence of both variables on the variable responses was demonstrated. The optimal conditions to obtain the highest degree of hydrolysis were enzyme/substrate ratio of 1.72% and 133 min of incubation. The highest radical scavenging activity (TEAC value of 2.7 ± 0.1 μmol Trolox equivalents/mg protein and ORAC value of 3.8 ± 0.1 μmol Trolox equivalents/mg protein) was found in hydrolyzates with alcalase after 138 min and an enzyme/substrate ratio of 1.87%. Peptides released by the action of alcalase and containing hydrophobic and aromatic amino acids could contribute to the antioxidant effects observed. Tarwi proteins could be a new alternative as a food additive with antioxidant properties or as an ingredient of functional foods for health promotion and prevention of free radical-induced chronic diseases.