Production and Characterization of Medium-Sized and Short Antioxidant Peptides from Soy Flour-Simulated Gastrointestinal Hydrolysate.

Chiara Cavaliere,Carmela Maria Montone,Paola Cuomo,Susy Piovesana,Anna Laura Capriotti,Aldo Laganà,Andrea Cerrato,Angela Michela Immacolata Montone,Rosanna Capparelli,Sara Elsa Aita

doi:10.3390/antiox10050734

Abstract

Soybeans (Glycine max) are an excellent source of dietary proteins and peptides with potential biological activities, such as antihypertensive, anti-cholesterol, and antioxidant activity; moreover, they could prevent cancer. Also, soy contains all the essential amino acids for nutrition; therefore, it represents an alternative to animal proteins. The goal of this paper was the comprehensive characterization of medium-sized and short peptides (two to four amino acids) obtained from simulated gastrointestinal digestion. Two different analytical approaches were employed for peptide characterization, namely a common peptidomic analysis for medium-sized peptides and a suspect screening analysis for short peptides, employing an inclusion list of exact m/z values of all possible amino acid combinations. Moreover, fractionation by preparative reversed-phase liquid chromatography was employed to simplify the starting protein hydrolysate. Six fractions were collected and tested for antioxidative activity by an innovative antioxidant assay on human gastric adenocarcinoma AGS cell lines. The two most active fractions (2 and 3) were then characterized by a peptidomic approach and database search, as well as by a suspect screening approach, in order to identify potential antioxidant amino acid sequences. Some of the peptides identified in these two fractions have been already reported in the literature for their antioxidant activity.

Highlights

In the last few decades, the opportunity to prevent, alleviate, or even treat some diseases by assuming functional food or bioactive compounds obtained from food is gaining increasing interest for both researchers and consumers
It is known that certain amino acid sequences can have one or more biological functions; for this reason, many studies are focused on the identification of bioactive peptides, which can be naturally present in food or can be obtained from the parent protein in which they are encrypted [1,2]
Compared to fraction 3, fraction 2 exhibited a higher protective effect against oxidative stress induced by H2 O2, almost returning the cells to the control group. These results suggest that soybean peptides have important antioxidant activities, with particular attention to peptides contained in fraction 2

Summary

Introduction

In the last few decades, the opportunity to prevent, alleviate, or even treat some diseases by assuming functional food or bioactive compounds obtained from food is gaining increasing interest for both researchers and consumers. It is known that certain amino acid sequences can have one or more biological functions; for this reason, many studies are focused on the identification of bioactive peptides, which can be naturally present in food or can be obtained from the parent protein in which they are encrypted [1,2]. These bioactive peptides are generally 2–20 amino acids long, Antioxidants 2021, 10, 734. To better simulate the physiological conditions in which peptides are formed from proteins, human digestive enzymes, which are found in the stomach, intestines, and pancreas (e.g., pepsin, trypsin, chymotrypsin, and pancreatin) can be used [5]

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