Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation Method
In this study, sodium caseinate (NaCas), soy protein isolate (SPI), and whey protein isolate (WPI) were used as structural materials for the delivery of rutin, naringenin, curcumin, hesperidin, and catechin. For each polyphenol, the protein solution was brought to alkaline pH, and then the polypheno...
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MDPI AG
2023-04-01
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Online Access: | https://www.mdpi.com/1420-3049/28/8/3573 |
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author | Ali Rashidinejad Matthijs Nieuwkoop Harjinder Singh Geoffrey B. Jameson |
author_facet | Ali Rashidinejad Matthijs Nieuwkoop Harjinder Singh Geoffrey B. Jameson |
author_sort | Ali Rashidinejad |
collection | DOAJ |
description | In this study, sodium caseinate (NaCas), soy protein isolate (SPI), and whey protein isolate (WPI) were used as structural materials for the delivery of rutin, naringenin, curcumin, hesperidin, and catechin. For each polyphenol, the protein solution was brought to alkaline pH, and then the polyphenol and trehalose (as a cryo-protectant) were added. The mixtures were later acidified, and the co-precipitated products were lyophilized. Regardless of the type of protein used, the co-precipitation method exhibited relatively high entrapment efficiency and loading capacity for all five polyphenols. Several structural changes were seen in the scanning electron micrographs of all polyphenol–protein co-precipitates. This included a significant decrease in the crystallinity of the polyphenols, which was confirmed by X-ray diffraction analysis, where amorphous structures of rutin, naringenin, curcumin, hesperidin, and catechin were revealed after the treatment. Both the dispersibility and solubility of the lyophilized powders in water were improved dramatically (in some cases, >10-fold) after the treatment, with further improvements observed in these properties for the powders containing trehalose. Depending on the chemical structure and hydrophobicity of the tested polyphenols, there were differences observed in the degree and extent of the effect of the protein on different properties of the polyphenols. Overall, the findings of this study demonstrated that NaCas, WPI, and SPI can be used for the development of an efficient delivery system for hydrophobic polyphenols, which in turn can be incorporated into various functional foods or used as supplements in the nutraceutical industry. |
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spelling | doaj.art-53e0734f0c184720855047dff49d9f9d2023-11-17T20:40:57ZengMDPI AGMolecules1420-30492023-04-01288357310.3390/molecules28083573Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation MethodAli Rashidinejad0Matthijs Nieuwkoop1Harjinder Singh2Geoffrey B. Jameson3Riddet Institute, Massey University, Private Bag 11 222, Palmerston North 4442, New ZealandRiddet Institute, Massey University, Private Bag 11 222, Palmerston North 4442, New ZealandRiddet Institute, Massey University, Private Bag 11 222, Palmerston North 4442, New ZealandRiddet Institute, Massey University, Private Bag 11 222, Palmerston North 4442, New ZealandIn this study, sodium caseinate (NaCas), soy protein isolate (SPI), and whey protein isolate (WPI) were used as structural materials for the delivery of rutin, naringenin, curcumin, hesperidin, and catechin. For each polyphenol, the protein solution was brought to alkaline pH, and then the polyphenol and trehalose (as a cryo-protectant) were added. The mixtures were later acidified, and the co-precipitated products were lyophilized. Regardless of the type of protein used, the co-precipitation method exhibited relatively high entrapment efficiency and loading capacity for all five polyphenols. Several structural changes were seen in the scanning electron micrographs of all polyphenol–protein co-precipitates. This included a significant decrease in the crystallinity of the polyphenols, which was confirmed by X-ray diffraction analysis, where amorphous structures of rutin, naringenin, curcumin, hesperidin, and catechin were revealed after the treatment. Both the dispersibility and solubility of the lyophilized powders in water were improved dramatically (in some cases, >10-fold) after the treatment, with further improvements observed in these properties for the powders containing trehalose. Depending on the chemical structure and hydrophobicity of the tested polyphenols, there were differences observed in the degree and extent of the effect of the protein on different properties of the polyphenols. Overall, the findings of this study demonstrated that NaCas, WPI, and SPI can be used for the development of an efficient delivery system for hydrophobic polyphenols, which in turn can be incorporated into various functional foods or used as supplements in the nutraceutical industry.https://www.mdpi.com/1420-3049/28/8/3573bioactive deliveryfood-grade proteinspolyphenolshydrophobic polyphenolspolyphenol–protein co-precipitationfunctional foods |
spellingShingle | Ali Rashidinejad Matthijs Nieuwkoop Harjinder Singh Geoffrey B. Jameson Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation Method Molecules bioactive delivery food-grade proteins polyphenols hydrophobic polyphenols polyphenol–protein co-precipitation functional foods |
title | Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation Method |
title_full | Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation Method |
title_fullStr | Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation Method |
title_full_unstemmed | Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation Method |
title_short | Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation Method |
title_sort | assessment of various food proteins as structural materials for delivery of hydrophobic polyphenols using a novel co precipitation method |
topic | bioactive delivery food-grade proteins polyphenols hydrophobic polyphenols polyphenol–protein co-precipitation functional foods |
url | https://www.mdpi.com/1420-3049/28/8/3573 |
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