Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance

Peng, Xinyan; Xiong, Youling L.; Kong, Baohua

doi:10.1016/j.foodchem.2008.07.068

Cited by 229 publications

(138 citation statements)

References 26 publications

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“…DPPH is a stable radical that shows maximal absorbance at 517 nm in ethanol (Molyneux, 2004). When the radical is scavenged by accepting an electron or a proton (H + ) from the antioxidant, the radical changes its color from purple to yellow and the absorbance is reduced (Peng et al, 2009). In the present study, collagen hydrolysates are the substances that donate an electron or hydrogen to neutralize the DPPH radical converting it into a stable molecule (Liu et al, 2010).…”

Section: Antioxidant Activitymentioning

confidence: 79%

In vitro antioxidant, antimutagenic and antiproliferative activities of collagen hydrolysates of jumbo squid (Dosidicus gigas) byproducts

et al. 2015

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Hydrolysates from two different jumbo squid byproducts (fins and arms), produced by trypsin and protease type XIV were compared on the basis of their antioxidant (DPPH and ABTS radical scavenging assays), antimutagenic (Ames test) and antiproliferative (Transformation cell proliferation in M12.C3F6 murine cells) activities. Jumbo squid arms had higher content of collagen than fins, and their hydrolysates had the highest antioxidant activity. Also, jumbo squid arm-derived collagen hydrolyzed with protease XIV showed the highest antimutagenic activity. The four hydrolysates obtained showed low antiproliferative activity, however they are susceptible for further studies to be applied as food additives.

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Section: Antioxidant Activitymentioning

confidence: 79%

In vitro antioxidant, antimutagenic and antiproliferative activities of collagen hydrolysates of jumbo squid (Dosidicus gigas) byproducts

et al. 2015

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“…As to samples 4, 5, 6 and 7, no band can be discriminated probably because of the extent of hydrolysis reaction (Table 1) forming small peptides which could have escaped the gel pore. According to Peng et al [45], hydrolysis percentage of whey protein isolate after 5 hours of enzymatic hydrolysis with Alcalase was of 35% -36%, which is a little bit higher than sample 4 percentage of hydrolysis. In such study, this percentage increased in the first 3 hours reaching a plateau at 5 hours.…”

Section: Optimization Of the Hydrolysis Processmentioning

confidence: 95%

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin

Fernández‑Fernández¹,

López-Pedemonte²,

Medrano-Fernández³

2017

FNS

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Whey proteins are known for their high nutritional value and bioactivity, notably great potential is found on α-lactalbumin. The objective of this study was to evaluate antioxidant, antiglycant and ACE (angiotensin converting enzyme)-inhibitory activity of α-lactalbumin peptides obtained from enzymatic hydrolysis with Alcalase through different hydrolysis conditions. The optimization of enzymatic hydrolysis was studied by response surface methodology variating enzyme:substrate ratio (0.0050%, 0.0525% and 0.1000% w/w) and time (0, 30 and 60 minutes) measuring antioxidant activity by ABTS and ORAC-FL (response variables), founding an augment of this activity with time. Characterization of seven samples showed increasing hydrolysis with time. Hydrolysate obtained with 0.1000% w/w and 60 minutes demonstrated higher antioxidant activity related to greater hydrolysis. This hydrolysate did not show antiglycant activity but promoted advanced glycation end products formation with methylglyoxal and glucose. In contrast, this sample showed 30% of ACE inhibition when compared to Captopril, having great potential by enhancing hydrolysis.

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“…It was also reported that when whey protein isolate (WPI) was hydrolyzed by Alcalase for 5 h, the prepared hydrolysates possessed the strongest antioxidant activity, and the inhibition of all WPI hydrolysates or fractions on DPPH radical ranged from 14.7% to 58.7% at 1 mg·mL −1 [21]. Compared to these results, casein hydrolysates of DH 9.6% prepared in our study showed a better ability to scavenge DPPH radical or ABTS ·+ , which was characterized by higher inhibition.…”

Section: Preparation Of Casein Hydrolysatesmentioning

confidence: 99%

Preparation and radical scavenging activity of papain-catalyzed casein plasteins

Zhao

2010

Dairy Sci. Technol.

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-The aim of this study was to prepare papain-catalyzed casein plasteins and to demonstrate the influence of the plastein reaction on the radical scavenging activity. Casein was initially hydrolyzed with papain under selected conditions to give a degree of hydrolysis of 9.6%. The casein hydrolysates were then subjected to papain-catalyzed plastein reaction to prepare casein plasteins. The formation of plasteins in the prepared casein plasteins was confirmed by size exclusion chromatography. The optimal conditions for the plastein reaction, determined by response surface methodology using the decrease of free amino groups in the casein plasteins as the response variable, were as follows: papain addition level was fixed at 500 U·g −1 proteins, reaction temperature 30°C, concentration of casein hydrolysates 50% and reaction time 5.6 h. Six different casein plasteins were prepared and the radical scavenging activity on two radicals, 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) (ABTS), was evaluated by the Trolox equivalent antioxidant capacity (TEAC). Analysis showed that all casein plasteins had improved radical scavenging activities. Compared to casein hydrolysates, the scavenging activity of the casein plasteins on DPPH radical had a seven-or ninefold increase, as TEAC increased from 10.45 to 73.41 or 90.31 mmol·g −1 proteins, while a onefold increase was detected on ABTS + (TEAC increased from 8.33 μmol·g −1 to 15.09 or 16.45 μmol·g −1 proteins). The results of this study clearly showed that the papain-catalyzed plastein reaction could be applied to prepare casein antioxidant peptides with higher activity, and that the plastein reaction may have a new application in dairy science.casein / plastein reaction / papain / radical scavenging activity / antioxidant 摘要 -酪蛋白类蛋白物的木瓜蛋白酶法制备及其自由基清除活性○ 本研究利用木瓜蛋白酶催化制备酪蛋白类蛋白物，证明类蛋白反应影响酪蛋白类蛋白物的自由基清除活性○ 首先，在选定的条件下用木瓜蛋白酶水解酪蛋白，制备出水解度为 9.6% 的酪蛋白水解物; 然后，酪蛋白水解物进行类蛋白反应制备酪蛋白类蛋白物，并且用排阻色谱证实所制备的酪蛋白类蛋白物中有类蛋白形成○ 优化的类蛋白反应条件，通过以酪蛋白类蛋白物的游离氨基含量降低为指标、利用响应面法而确定，它们分别是: 木瓜蛋白酶添加量固定为每克蛋白质 500 U，反应温度为 30°C，酪蛋白水解物质量分数为 50%，反应时间为 5.6 h○ 制备 6 个反应程度不同的酪蛋白类蛋白物，并评价它们对 2 个自由基 1,1-二苯基-2-苦基肼 (DPPH)、2,2'-连氮-二 (3-乙基-苯并噻唑啉-6-磺酸)(ABTS) 的 Trolox 等价抗氧化能力 (TEAC)○ 分析结果显示，所有的酪蛋白类蛋白物的自由基清除活性得到改善○ 与酪 Résumé -Préparation de plastéines à partir de la catalyse de caséines par la papaïne et leur activité anti-radicalaire. L'objectif de cette étude était de préparer des plastéines à partir de la catalyse de caséines par la papaïne et de démontrer l'influence de la réaction de formation des plastéines sur l'activité anti-radicalaire. La caséine a été préalablement hydrolysée par la papaïne dans des conditions sélectionnées afin d'obtenir un degré d'hydrolyse de 9,6 %. Les hydrolysats de caséine ont ensuite été soumis à une réaction de catalyse par la papaïne pour préparer les plastéines. La formation des plastéines a été confirmée par chromatographie d'exclusion de taille. Les conditions optimales de la réaction, déterminées par la méthode de surface de réponse ...

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Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance

Cited by 229 publications

References 26 publications

In vitro antioxidant, antimutagenic and antiproliferative activities of collagen hydrolysates of jumbo squid (Dosidicus gigas) byproducts

In vitro antioxidant, antimutagenic and antiproliferative activities of collagen hydrolysates of jumbo squid (Dosidicus gigas) byproducts

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin

Preparation and radical scavenging activity of papain-catalyzed casein plasteins

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Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance

Cited by 229 publications

References 26 publications

In vitro antioxidant, antimutagenic and antiproliferative activities of collagen hydrolysates of jumbo squid (Dosidicus gigas) byproducts

In vitro antioxidant, antimutagenic and antiproliferative activities of collagen hydrolysates of jumbo squid (Dosidicus gigas) byproducts

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of &lt;i&gt;α&lt;/i&gt;-Lactalbumin

Preparation and radical scavenging activity of papain-catalyzed casein plasteins

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Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin