Antioxidant activities of enzymatic‐hydrolysed proteins of dromedary (<i>Camelus dromedarius</i>) colostrum

Oussaief, Olfa; Jrad, Zeineb; Adt, Isabelle; Dbara, Mohamed; Khorchani, Touhami; El‐Hatmi, Halima

doi:10.1111/1471-0307.12668

Cited by 14 publications

(11 citation statements)

References 27 publications

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“…What is more, there is a significant positive correlation between hydrolysis time and the DPPH radical scavenging activity of WPH. Our study is in agreement with the study by OLFAOUSSAIEF, where the antioxidant activity of all dromedary colostrum hydrolysates were significantly more effective than single peak colostrum proteins [ 28 ]. Similarly, Zheng et al [ 21 ] demonstrated that the rate of free radical scavenging decreased with increasing hydrolysis, indicating a negative correlation between DH and DPPH free radical scavenging activity in oat protein hydrolysis products.…”

Section: Resultssupporting

confidence: 93%

Purification, Identification and Molecular Docking of Novel Antioxidant Peptides from Walnut (Juglans regia L.) Protein Hydrolysates

Fan

Mao

2022

Molecules

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Walnut protein isolate (WPI) was hydrolyzed using Alcalase for 0, 30, 60, 90, 120 and 150 min to investigate the effect of different hydrolysis times on the structure and antioxidant properties of walnut proteins. The identified peptides HADMVFY, NHCQYYL, NLFHKRP and PSYQPTP were used to investigate the structure-activity relationship by using LC-MS/MS and molecular docking. The kinetic equations DH = 3.72ln [1 + (6.68 E0/S0 + 0.08) t] were developed and validated to explore the mechanism of WIP hydrolysis by Alcalase. Structural characteristics showed that the UV fluorescence intensity and endogenous fluorescence intensity of the hydrolysates were significantly higher than those of the control. FTIR results suggested that the secondary structure gradually shifted from an ordered to a disordered structure. Enzymatic hydrolysis containing much smaller molecule peptides than WPI was observed by molecular weight distribution. In vitro, an antioxidant test indicated that Alcalase protease hydrolysis at 120 min showed more potent antioxidant activity than hydrolysates at other hydrolysis times. In addition, four new antioxidant peptides were identified by LC-MS/MS. Molecular docking indicated that these peptides could interact with ABTS through interactions such as hydrogen bonding and hydrophobic interactions. Thus, WPI hydrolysates could be used as potential antioxidants in the food and pharmaceutical industries.

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Section: Resultssupporting

confidence: 93%

Purification, Identification and Molecular Docking of Novel Antioxidant Peptides from Walnut (Juglans regia L.) Protein Hydrolysates

Fan

Mao

2022

Molecules

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Section: Resultssupporting

confidence: 88%

“…The IC 50 values for the other hydrolysates were between 0.437 and 0.836 mg/ mL. These results are in agreement with the hydrolysates from dromedary colostrum proteins (16). However, Oh et al (40) reported higher IC 50 values for cow's milk protein hydrolysates than those in the present study.…”

Section: Effects Of Enzymatic Hydrolysis On the Antioxidant Activities Of Dromedary Milk Proteinssupporting

confidence: 90%

“…Dromedary milk protein hydrolysis was performed as described by Oussaief et al . ( 16 ) with slight modifications. Dromedary skimmed milk was resuspended on protein basis at 2.5% ( m/V ) in ultrapure water and the pH of this solution was adjusted to the optimal pH value of enzymes: 2 for pepsin, 8 for trypsin, α-chymotrypsin, pancreatin and pronase and 6.5 for papain, as given by the manufacturer.…”

Section: Methodsmentioning

confidence: 99%

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Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

Oussaief

Jrad

Adt

et al. 2020

Food technol. biotechnol. (Online)

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Research background. Milk protein hydrolysates have received particular attention due to their health-promoting effects. Dromedary milk differs from the milk of other dairy animals in the composition and structure of its protein components, which give it unique properties. The bioactivity and functionality of whole dromedary milk proteins and their enzymatic hydrolysates have not received much attention, hence this study aims to investigate the effect of enzymatic hydrolysis of dromedary milk proteins on their antioxidant activities and functional properties. Experimental approach. Dromedary milk proteins were treated using four proteolytic enzymes (pepsin, trypsin, α-chymotrypsin and papain) and two mixtures of enzymes (pancreatin and pronase). The degree of hydrolysis was measured to verify the hydrolysis of the proteins. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography served to determine the molecular mass distribution of the hydrolysates while reversed phase-high performance liquid chromatography (RP-HPLC) was conducted to explore their hydrophobicity. The antioxidant activities were evaluated using various in vitro tests, including 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical scavenging capacities, iron(III) reducing ability and chelating activity. Besides, functional properties such as solubility, foaming and emulsification were assessed. Results and conclusions. Dromedary milk protein hydrolysates exhibited different degrees of hydrolysis ranging from 17.69 to 41.86 %. Apart from that, the hydrolysates showed different electrophoretic patterns, molecular mass distribution and RP-HPLC profiles demonstrating the heterogeneity of the resulting peptides in terms of molecular mass and polarity. The hydrolysates displayed significantly higher antioxidant capacities than the undigested proteins at all the tested concentrations. Iron(II) chelating activity was the most improved assay after proteolysis and the hydrolysate generated with pancreatin had the highest chelating power. Dromedary milk protein hydrolysates possessed good solubility (>89 %). Further, foaming and emulsifying properties of dromedary milk proteins were enhanced after their proteolysis. These interfacial properties were influenced by the enzymes employed during proteolysis. Novelty and scientific contribution. Enzymatic hydrolysis of dromedary milk proteins is an effective tool to obtain protein hydrolysates with great antioxidant and functional properties. These results suggest that dromedary milk protein hydrolysates could be used as a natural source of antioxidant peptides to formulate functional foods and nutraceuticals.

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“…This specific composition of colostrum may reveal particular biological activities. Antioxidant activity is among the fundamental biological activities important for life (Oussaief et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

Physicochemical and sensory evaluation of greek style yoghurt with bovine colostrum

et al. 2022

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This study aimed to develop Greek style yoghurts with the addition of bovine colostrum. Four yoghurt formulations were produced with different colostrum content (0%, 10%, 20% and 30%). The fat, protein, total solids, ash, retinol levels were quantified as well as the colour was measured. A sensory analysis was conducted with 103 untrained panelists, evaluating the attributes of appearance, aroma, consistency, flavour, overall acceptance and the purchase intention. Colostrum addition increased the fat and protein levels in the yoghurt formulations. The Greek style yoghurts with bovine colostrum reached sensory acceptance above 70% for all attributes.

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Antioxidant activities of enzymatic‐hydrolysed proteins of dromedary (Camelus dromedarius) colostrum

Cited by 14 publications

References 27 publications

Purification, Identification and Molecular Docking of Novel Antioxidant Peptides from Walnut (Juglans regia L.) Protein Hydrolysates

Purification, Identification and Molecular Docking of Novel Antioxidant Peptides from Walnut (Juglans regia L.) Protein Hydrolysates

Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

Physicochemical and sensory evaluation of greek style yoghurt with bovine colostrum

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