Abstract:It has been estimated and demonstrated that the antioxidant capacity of proteins is increased as a result of digestion in the gastrointestinal tract, which can be contributed by denaturation and digestion. This study aimed to evaluate the effect of denaturation and proteolytic digestion on the antioxidant activity of bovine serum albumin (BSA) and chicken egg white proteins in model systems. Denaturation with an anionic detergent (sodium dodecyl sulfate) and digestion with papain and trypsin increased the anti… Show more
“…The color disappeared gradually after ~10 min, presumably decomposed via redox cycling. Differences in the spectra of the laccase-ABTS • adduct (λ max = 575 nm) and for the tyrosine-ABTS adduct (λ max = 555 nm) of ABTS • and free tyrosine formed in a reaction catalyzed by laccase were ascribed to the influence of the protein environment [18]. The reaction of ABTS with lipocalin α1-microglobulin, also leading to the formation of a purple product, conditioned by the formation of ABTSadducts to at least two tyrosine residues in the protein molecule, was also reported [19].…”
Section: Discussionmentioning
confidence: 99%
“…Tyrosine residues are one of the amino acid residues most susceptible to oxidative modifications, including one-electron oxidations [23]. Tyrosine radicals, if formed in proteins, are able to form adducts with various radicals [18]. Tyrosine nitration proceeds via the formation of tyrosyl radicals and the subsequent reaction of these radicals with • NO 2 .…”
The reaction of the 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) free radical (ABTS●) with proteins (bovine serum albumin, blood plasma, egg white, erythrocyte membranes, and Bacto Peptone) leads not only to a reduction of ABTS● but also to the appearance of a purple color (absorption maximum at 550–560 nm). The aim of this study was to characterize the formation and explain the nature of the product responsible for the appearance of this color. The purple color co-precipitated with protein, and was diminished by reducing agents. A similar color was generated by tyrosine upon reaction with ABTS●. The most feasible explanation for the color formation is the addiction of ABTS● to proteins’ tyrosine residues. The product formation was decreased by nitration of the bovine serum albumin (BSA) tyrosine residues. The formation of the purple product of tyrosine was optimal at pH 6.5. A decrease in pH induced a bathochromic shift of the spectra of the product. The product was not a free radical, as demonstrated by electrom paramagnetic resonance (EPR) spectroscopy. Another byproduct of the reaction of ABTS● with tyrosine and proteins was dityrosine. These byproducts can contribute to the non-stoichiometry of the antioxidant assays with ABTS●. The formation of the purple ABTS adduct may be a useful index of radical addition reactions of protein tyrosine residues.
“…The color disappeared gradually after ~10 min, presumably decomposed via redox cycling. Differences in the spectra of the laccase-ABTS • adduct (λ max = 575 nm) and for the tyrosine-ABTS adduct (λ max = 555 nm) of ABTS • and free tyrosine formed in a reaction catalyzed by laccase were ascribed to the influence of the protein environment [18]. The reaction of ABTS with lipocalin α1-microglobulin, also leading to the formation of a purple product, conditioned by the formation of ABTSadducts to at least two tyrosine residues in the protein molecule, was also reported [19].…”
Section: Discussionmentioning
confidence: 99%
“…Tyrosine residues are one of the amino acid residues most susceptible to oxidative modifications, including one-electron oxidations [23]. Tyrosine radicals, if formed in proteins, are able to form adducts with various radicals [18]. Tyrosine nitration proceeds via the formation of tyrosyl radicals and the subsequent reaction of these radicals with • NO 2 .…”
The reaction of the 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) free radical (ABTS●) with proteins (bovine serum albumin, blood plasma, egg white, erythrocyte membranes, and Bacto Peptone) leads not only to a reduction of ABTS● but also to the appearance of a purple color (absorption maximum at 550–560 nm). The aim of this study was to characterize the formation and explain the nature of the product responsible for the appearance of this color. The purple color co-precipitated with protein, and was diminished by reducing agents. A similar color was generated by tyrosine upon reaction with ABTS●. The most feasible explanation for the color formation is the addiction of ABTS● to proteins’ tyrosine residues. The product formation was decreased by nitration of the bovine serum albumin (BSA) tyrosine residues. The formation of the purple product of tyrosine was optimal at pH 6.5. A decrease in pH induced a bathochromic shift of the spectra of the product. The product was not a free radical, as demonstrated by electrom paramagnetic resonance (EPR) spectroscopy. Another byproduct of the reaction of ABTS● with tyrosine and proteins was dityrosine. These byproducts can contribute to the non-stoichiometry of the antioxidant assays with ABTS●. The formation of the purple ABTS adduct may be a useful index of radical addition reactions of protein tyrosine residues.
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