Production of Protein Hydrolysates Teff () Flour with Antioxidant and Angiotensin-I-Converting Enzyme (ACE-I) Inhibitory Activity Using Pepsin and L. Extract

Overview

Journal Curr Issues Mol Biol

Publisher MDPI

Specialty Molecular Biology

Date 2024 Oct 25

PMID 39451552

Authors

Gregorio Molina-Valero

Laura Buendia-Moreno

Cindy Bande-De Leon

Estefania Bueno-Gavila

Luis Tejada

Affiliations

Soon will be listed here.

Abstract

In recent years, several studies have shown the antioxidant and antihypertensive potential of bioactive peptides. Thus, bioactive peptides are likely to be a valuable substance for the development of functional foods. There are a wide variety of sources of these peptides, including several cereals. Teff is an Ethiopian-rooted cereal with an interesting nutritional profile, mainly due to its high amount of protein. In this study, teff flour was subjected to a defatting process for optimizing the protein extraction. Such extraction was performed by precipitation from its isoelectric point, a crucial step that separates the protein from other components based on their charge. The protein obtained was subjected to enzymatic hydrolysis by pepsin and L. The antihypertensive (angiotensin-I-converting enzyme -ACE-I- inhibitory activity) and antioxidant activity (2,2-diphenyl-1-picrylhydrazyl -DPPH- radical scavenging activity) of the peptides were determined. According to the IC values, the results obtained showed that the peptides from teff flour show promising bioactivity compared to other cereals. Furthermore, the peptides from teff flour obtained from L. showed higher antioxidant activity (defatted teff flour -DTF-: 0.59 ± 0.05; protein extract -EP- : 1.04 ± 0.11) than those obtained with pepsin (DTF: 0.87 ± 0.09; EP: 1.73 ± 0.11). However, L. hydrolyzate peptides showed lower inhibitory activity of ACE-I (DTF: 0.59 ± 0.07; EP: 0.61 ± 0.05) than the pepsin hydrolyzate (DTF: 0.15 ± 0.02; EP: 0.33 ± 0.05).

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