2020
DOI: 10.38212/2224-6614.2720
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Antioxidant activities of carnosine, anserine, some free amino acids and their combination

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Cited by 53 publications
(54 citation statements)
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“…The absorbance was measured at 485 nm and 520 nm to monitor the murexide-copper complex, and free murexide in solution, respectively. The absorbance ratio A 485 /A 520 was considered to be proportional to the amount of free Cu(II) concentration in solution [56,57].…”
Section: Copper(ii)-chelating Activitymentioning
confidence: 99%
See 1 more Smart Citation
“…The absorbance was measured at 485 nm and 520 nm to monitor the murexide-copper complex, and free murexide in solution, respectively. The absorbance ratio A 485 /A 520 was considered to be proportional to the amount of free Cu(II) concentration in solution [56,57].…”
Section: Copper(ii)-chelating Activitymentioning
confidence: 99%
“…In a first set of experiments, we evaluated the Fe(II) and the Cu(II) chelating ability of GQDs and compared the results with those that were obtained while using EDTA and carnosine, compounds that are well-known to exhibit metal chelating properties [53][54][55][56][57]. GQDs, used at various concentrations, were added to a 2 mM solution and FeCl 2 and the mixture was incubated for 3 min at room temperature.…”
Section: Fe(ii) and Cu(ii) Chelating Propertiesmentioning
confidence: 99%
“…Previous studies have focused on chicken essence when attributing anserine and carnosine's various antioxidative, antiglycating, anti-inflammation, antilipogenic, and antifatigue protective properties [3][4][5][6][7]. Others have only focused on carnosine's antioxidative role [8].…”
Section: Introductionmentioning
confidence: 99%
“…Despite EP‐digested caseins showed less DH than EM‐digested caseins, we found that the antioxidant activity of EP‐digested caseins was higher in all considered times than that obtained with the EM extract ( P < 0.05). Taking into account that the antioxidant activity during hydrolysis is affected by enzyme specificity that generates peptides and free amino acids with different size, level and composition (Wu et al , ), the explanation could be ascribed to the pepsin action, specific towards hydrophobic amino acids which, following cleavage, become exposed facilitating the transfer of electrons to the reactive oxygen species (Power et al , ). EM extract, on the other hand, is characterised by the presence of proteolytic enzymes with different cleavage sites which act simultaneously on the substrate, causing an increase in the DH over time, but also the probable release of low antioxidant capacity peptides and inactive peptides.…”
Section: Resultsmentioning
confidence: 99%