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Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

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 functi...

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Autores principales: Oussaief, Olfa, Jrad, Zeineb, Adt, Isabelle, Khorchani, Touhami, El-Hatmi, Halima
Formato: Online Artículo Texto
Lenguaje:English
Publicado: University of Zagreb Faculty of Food Technology and Biotechnology 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7416125/
https://www.ncbi.nlm.nih.gov/pubmed/32831567
http://dx.doi.org/10.17113/ftb.58.02.20.6337
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author Oussaief, Olfa
Jrad, Zeineb
Adt, Isabelle
Khorchani, Touhami
El-Hatmi, Halima
author_facet Oussaief, Olfa
Jrad, Zeineb
Adt, Isabelle
Khorchani, Touhami
El-Hatmi, Halima
author_sort Oussaief, Olfa
collection PubMed
description 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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spelling pubmed-74161252020-08-20 Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties Oussaief, Olfa Jrad, Zeineb Adt, Isabelle Khorchani, Touhami El-Hatmi, Halima Food Technol Biotechnol Original Scientific Papers 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. University of Zagreb Faculty of Food Technology and Biotechnology 2020-06 /pmc/articles/PMC7416125/ /pubmed/32831567 http://dx.doi.org/10.17113/ftb.58.02.20.6337 Text en http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC BY) 4.0 License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Scientific Papers
Oussaief, Olfa
Jrad, Zeineb
Adt, Isabelle
Khorchani, Touhami
El-Hatmi, Halima
Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties
title Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties
title_full Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties
title_fullStr Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties
title_full_unstemmed Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties
title_short Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties
title_sort dromedary milk protein hydrolysates show enhanced antioxidant and functional properties
topic Original Scientific Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7416125/
https://www.ncbi.nlm.nih.gov/pubmed/32831567
http://dx.doi.org/10.17113/ftb.58.02.20.6337
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