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Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels

Consumer demand for high protein content and plant-based fat has necessitated novel approaches to healthy food products. In response to this need, oleogels (OG) (structured liquid oils) emerged as a possible means of not only replacing saturated and trans fats but also delivering food protein. Never...

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Autores principales: Park, Clifford, Jimenez-Flores, Rafael, Maleky, Farnaz
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7699611/
https://www.ncbi.nlm.nih.gov/pubmed/33228228
http://dx.doi.org/10.3390/foods9111697
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author Park, Clifford
Jimenez-Flores, Rafael
Maleky, Farnaz
author_facet Park, Clifford
Jimenez-Flores, Rafael
Maleky, Farnaz
author_sort Park, Clifford
collection PubMed
description Consumer demand for high protein content and plant-based fat has necessitated novel approaches to healthy food products. In response to this need, oleogels (OG) (structured liquid oils) emerged as a possible means of not only replacing saturated and trans fats but also delivering food protein. Nevertheless, an in-depth view of the structure of networks made of OG and protein is deficient. Hence, the objective of this study is developing oleocolloid (OC) (whey protein and rice bran wax OG) and hydro-oleocolloid (HOC) (OC + water) matrices with varying protein content (2.5–7.5%) to characterize their structural properties. Thermal analysis of the matrices via differential scanning calorimetry (DSC) documented the effects of hydrophobic interactions on the protein structure and its stability. Whey protein denaturation temperature increased from 74.9 °C to 102.8 °C in the presence of high oleic soybean oil. The effects of vegetable oil on WPI structure was also verified by FTIR spectroscopy. Data analysis revealed slight structural changes of the WPI secondary structure in the hydrophobic oil medium and the α-helix and β-sheet proportion in the emulsion medium was significantly altered. Similar analysis was performed in OC and HOC networks to quantify possible interactions between protein and rice bran wax. Results indicated that the protein was denatured during the thermal and mechanical conditions required for the oleogelation process, while it did not affect the systems’ solid fat content (SFC) and polymorphic patterns of the oleogels. However, DSC analysis showed different onset of melting for OC and HOC samples due to colloidal interactions between the protein and the lipid phase. The role of these chemistry was confirmed by microscopy analyses where OC and HOC matrices displayed notably different microstructural properties. The observed differences in the structural properties between OC and HOC matrices indicate the different colloidal interactions mediated by oleogelation process and the liquid medium type (oil vs. emulsion).
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spelling pubmed-76996112020-11-29 Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels Park, Clifford Jimenez-Flores, Rafael Maleky, Farnaz Foods Article Consumer demand for high protein content and plant-based fat has necessitated novel approaches to healthy food products. In response to this need, oleogels (OG) (structured liquid oils) emerged as a possible means of not only replacing saturated and trans fats but also delivering food protein. Nevertheless, an in-depth view of the structure of networks made of OG and protein is deficient. Hence, the objective of this study is developing oleocolloid (OC) (whey protein and rice bran wax OG) and hydro-oleocolloid (HOC) (OC + water) matrices with varying protein content (2.5–7.5%) to characterize their structural properties. Thermal analysis of the matrices via differential scanning calorimetry (DSC) documented the effects of hydrophobic interactions on the protein structure and its stability. Whey protein denaturation temperature increased from 74.9 °C to 102.8 °C in the presence of high oleic soybean oil. The effects of vegetable oil on WPI structure was also verified by FTIR spectroscopy. Data analysis revealed slight structural changes of the WPI secondary structure in the hydrophobic oil medium and the α-helix and β-sheet proportion in the emulsion medium was significantly altered. Similar analysis was performed in OC and HOC networks to quantify possible interactions between protein and rice bran wax. Results indicated that the protein was denatured during the thermal and mechanical conditions required for the oleogelation process, while it did not affect the systems’ solid fat content (SFC) and polymorphic patterns of the oleogels. However, DSC analysis showed different onset of melting for OC and HOC samples due to colloidal interactions between the protein and the lipid phase. The role of these chemistry was confirmed by microscopy analyses where OC and HOC matrices displayed notably different microstructural properties. The observed differences in the structural properties between OC and HOC matrices indicate the different colloidal interactions mediated by oleogelation process and the liquid medium type (oil vs. emulsion). MDPI 2020-11-19 /pmc/articles/PMC7699611/ /pubmed/33228228 http://dx.doi.org/10.3390/foods9111697 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Park, Clifford
Jimenez-Flores, Rafael
Maleky, Farnaz
Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels
title Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels
title_full Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels
title_fullStr Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels
title_full_unstemmed Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels
title_short Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels
title_sort quantifications of oleocolloid matrices made of whey protein and oleogels
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7699611/
https://www.ncbi.nlm.nih.gov/pubmed/33228228
http://dx.doi.org/10.3390/foods9111697
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