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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doaj-f0b043c9614c4e74baf417f2d0bc7b672020-11-25T04:02:52ZengMDPI AGFoods2304-81582020-11-0191697169710.3390/foods9111697Quantifications of Oleocolloid Matrices Made of Whey Protein and OleogelsClifford Park0Rafael Jimenez-Flores1Farnaz Maleky2Department of Food Science and Technology, The Ohio State University, 2015 Fyffe Ct., Columbus, OH 43210, USADepartment of Food Science and Technology, The Ohio State University, 2015 Fyffe Ct., Columbus, OH 43210, USADepartment of Food Science and Technology, The Ohio State University, 2015 Fyffe Ct., Columbus, OH 43210, USAConsumer 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).https://www.mdpi.com/2304-8158/9/11/1697oleocolloidhydro-oleocolloidprotein denaturationhydrophobic interactionsstructuredispersion and solubilization |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Clifford Park Rafael Jimenez-Flores Farnaz Maleky |
spellingShingle |
Clifford Park Rafael Jimenez-Flores Farnaz Maleky Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels Foods oleocolloid hydro-oleocolloid protein denaturation hydrophobic interactions structure dispersion and solubilization |
author_facet |
Clifford Park Rafael Jimenez-Flores Farnaz Maleky |
author_sort |
Clifford Park |
title |
Quantifications of Oleocolloid Matrices Made of Whey Protein and Oleogels |
title_short |
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_sort |
quantifications of oleocolloid matrices made of whey protein and oleogels |
publisher |
MDPI AG |
series |
Foods |
issn |
2304-8158 |
publishDate |
2020-11-01 |
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). |
topic |
oleocolloid hydro-oleocolloid protein denaturation hydrophobic interactions structure dispersion and solubilization |
url |
https://www.mdpi.com/2304-8158/9/11/1697 |
work_keys_str_mv |
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