Small peptides and free amino acids have the advantage of being absorbed in the intestine without any digestion in the stomach. This explains their use in many formulas such as diets for nursing infants or sick adults and as stimulants for people liable for allergy development. The production of peptides through hydrolytic reactions seems to be the most promising technique to form proteinaceous antioxidants since peptides have higher antioxidant activity than raw proteins. In the present study, proteins extracted from flours of peas and lupin were hydrolyzed with microbial enzymes from whole cells of Lactobacillus fermentum MR13 and Lactobacillus rhamnosus C249. The products of the hydrolysis further separated by Size Exclusion Chromatography and the main fractions purified were analyzed for their antioxidant activity by DPPH assay. The results showed that both the total fractions, both the single fractions enhanced the antioxidant activity of the not hydrolyzed substrates. The antioxidant activities of hydrolyzed vegetal proteins seemed to be in relation to their molecular weight distribution. The peptides present in the fractions with highest antioxidant activity were identified with nanoLC-qTOF MS/MS analysis. As emerged from the present study, hydrolyzed vegetal proteins have the potential to become good ingredients and supplements in new food formulas.
|Data di pubblicazione:||2013|
|Autori:||L. Dei Più; D. Tagliazucchi; E. Babini; A. Gianotti|
|Titolo:||Hydrolysis of pea and lupin proteins by microorganisms to produce bioactive peptides|
|Appare nelle tipologie:||Abstract in Atti di Convegno|
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