Purification and Characterization of Antioxidant Peptides From Soy Protein Hydrolysate

Abstract

Soy protein hydrolysates (SPH) were obtained by Alcalase hydrolysis of soy protein. Antioxidant activity of SPH was measured with a lipid peroxidation inhibitory activity and lipid oxidation was evaluated by measuring the thiobarbituric acid (TBA) and peroxide value. The potent antioxidant peptide was purified using ultrafiltration and consecutive chromatographic methods including FPLC and reverse‐phase high‐performance liquid chromatography. The antioxidant activity having a specific activity of 108.13%/µg for TBA method was enhanced 67.6‐fold compared with SPH. In the amino acid composition of the final potent antioxidant peptide, hydrophobic amino acids were the most abundant amino acids and among them phenylalanine was especially abundant. PRACTICAL APPLICATIONS Soybean is important because of not only its multiple health‐promoting properties but also its role as a useful source for producing biological active peptides. Enzymatic hydrolysis has been employed in order to produce the active peptide from various protein sources because of its naturalness and safety. In this paper, the potent antioxidant peptide was purified by an ultrafiltration and a series of chromatography from soy protein hydrolysates (SPH) obtained by Alcalase treatment. It is expected that the SPH with enhanced antioxidant activity could be used in a wide range of foods as a useful functional food ingredient.

Fractionation, Separation, and Identification of Antioxidative Peptides in Potato Protein Hydrolysate that Enhance Oxidative Stability of Soybean Oil Emulsions

“…Most of the identified peptides were in the 500 to 900 Da range that corresponded to 5 to 7 amino acid residues, in agreement with literature reports that bioactive peptides generally consist of 2 to 9 amino acids (Kitts and Weiler 2003). In addition to the molecular size, hydrophobicity of peptides, or the proportion of hydrophobic amino acids present in peptides, is widely reported to correlate with peptide antioxidant activity (Byun and others 2009; Park and others 2010; Pownall and others 2010; Tang and others 2010). In the 6 identified peptides in the present study, there was no prevalent amino acid.…”

A Comprehensive Review of Corn Protein‐derived Bioactive Peptides: Production, Characterization, Bioactivities, and Transport Pathways

“…FPLC, such as gel permeation chromatography or ion-exchange (IEX) columns, is used for the separation and enrichment of the initial hydrolysates (Bougatef et al, 2008;Sanghoon, Qian, & Sekwon, 2010). The main product undergoes further separation into specific peptide fractions by reverse-phase high-performance liquid chromatography (RP-HPLC), DEAE-sepharose fast-flow or size-exclusion chromatography (Amiot et al, 2004;Jian, Zheng, Liu, & Liu, 2010;Moayedi et al, 2017;Sun et al, 2012). For example, to prepare diverse bioactive CPs, the hydrolysis can be subjected to ceramic/regenerated cellulose membranes of various MWs, and then the mineral salts and free amino acids are eliminated via NF Yu et al, 2012).…”

“…Various studies have been conducted to research the antioxidant properties of hydrolysates from natural protein sources, especially from plant sources such as corn protein (Jin et al, 2016;, rapeseed protein hydrolysates Mu, Jiang, & Pan, 2011), and sunflower protein (Jian et al, 2010), chickpea albumin (Kou et al, 2013) as well as some animal proteins such as rotifers (Byun, Lee, Park, Jeon, & Kim, 2009), porcine hemoglobin , and blue mussel (Rajapakse et al, 2005).…”

Antihypertensive Properties of Plant Protein Derived Peptides

“…Purification of peptide by ultrafiltration and chromatographic techniques enhanced the specific activity 67.9-fold compared to hydrolysate. The final potent antioxidant peptide contained hydrophobic amino acids and among them, Phe was especially abundant [141].…”