Antioxidant activity ofVigna unguiculataL. walp and hard-to-cookPhaseolus vulgarisL. protein hydrolysates

Abstract

Recent research, using model systems, has shown that enzymatic hydrolysis of food proteins can make them act as direct scavengers of diverse free radicals. This study aimed at the characterization of protein hydrolysates with antioxidant properties from Vigna unguiculata L. walp and hard-to-cook Phaseolus vulgaris L. protein concentrates. The maximum values obtained for all the assays were 15.1 mM/mg of protein for Trolox-equivalent-antioxidative capacity, 98.2% for percentage of 2,2-diphenyl-1-picrylhydrazyl (DPPH) discoloration, 70.1% and 71.4% for iron and copper chelating activities, respectively. The reducing power of hydrolysates was higher than butylated hydroxytoluene (BHT) (control). The antioxidant activity of the hydrolysates may be a result of enzymatic hydrolysis generating peptides that exhibit this type of activity. The hydrolysates showed an increase of amino acids that have been associated with the biological activity of peptides with antioxidant activity, such as hydrophobic residues: Ala, Phe and Ile; hydrophilic: Lys and neutral: Ser and Gly.Keywords: Vigna unguiculata; Phaseolus vulgaris; hydrolysates; antioxidant activity Estudios recientes han demostrado que los hidrolizados enzima´ticos de proteı´nas alimentarias pueden actuar directamente sobre radicales libres. El objetivo del presente trabajo fue caracterizar las propiedades antioxidantes de hidrolizados proteı´nicos de Vigna unguiculata L. walp y Phaseolus vulgaris L. endurecido. Los valores ma´ximos obtenidos para las determinaciones efectuadas fueron, 15,1 mM/mg de proteı´na de Capacidad Antioxidante Equivalente de Trolox, 98,2% de decoloracio´n del radical DPPH, 70,1% y 70,4% de capacidad quelante de cobre y hierro, respectivamente. El poder reductor de los hidrolizados fue superior al del BHT (control). La capacidad antioxidante posiblemente se relacione conlos pe´ptidos generados durante la hidrolisis, los cuales presentan dicha actividad. La composicio´n aminoacı´dica de los hidrolizados mostro´un incremento de aminoa´cidos hidrofo´bicos (Ala, Fen e Ile), hidrofı´licos (Lis) y neutros (Ser y Gli), los cuales han sido asociados a la secuencia de pe´ptidos con actividad antioxidantes.

Antioxidant Potential of Mung Bean (Vigna radiata) Albumin Peptides Produced by Enzymatic Hydrolysis Analyzed by Biochemical and In Silico Methods

“…Mung bean albumin peptides showed high ferrous ion chelating activity, but low ABTS radical scavenging activity (Supplementary Materials Figure S1). The ferrous ion chelating activity of mung bean albumin peptides derived from pepsin-pancreatin enzymatic hydrolysis was found to be higher than the ferrous ion chelating activity of cowpea and common bean protein hydrolysates derived from the same enzyme scheme, as reported by Segura-Campos et al [36]. The ferrous ion chelating activity of mung bean albumin peptides was also found to be higher than the ferrous ion chelating activity of soybean lunasin, as reported by Garcia-Nebot et al [37].…”

Isolation and Identification of Tyrosinase-Inhibitory and Copper-Chelating Peptides from Hydrolyzed Rice-Bran-Derived Albumin

“…These amino acids have been reported to contribute to tyrosinase-inhibition and metal-chelating activity. 1,17,19,22,23,24,46…”

“…Several researchers have reported the tyrosinase-inhibitory effect and copper-chelating activity of proteins, protein hydrolysates, and peptides from natural sources such as rice bran, 2,16 silk, 17 sunflower, 18 zein, 19 chickpea, 20,21 cowpea, 22 and red seaweed. 23 Some synthetic short peptides appear to show inhibitory activity against tyrosinase.…”

Improving antioxidant activity of black bean protein by hydrolysis with protease combinations

“…Segura‐Campos et al . () studied the use of the mixture of Flavourzyme and Alcalase on the enzymatic hydrolysis of hard‐to‐cook bean protein concentrates and demonstrated that the combined use of these enzymes was able to increase the antioxidant activity of the hydrolysates.…”