Impact of heating treatments on physical stability and lipid-protein co-oxidation in oil-in-water emulsion prepared with soy protein isolates

Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products

“…These results proved that MDA may cause more serious unfolding of the unadsorbed and adsorbed proteins compared with the 13-HPODE at relatively higher addition levels. Additionally, Li et al [ 19 ] indicated that the structural changes of soy protein isolate induced by lipid oxidation could obviously increase the droplet size of O/W emulsions during storage, indicated by clear flocculation and creaming. However, due to the higher melting point (33.3 °C) of fully hydrogenated coconut oil [ 28 ], droplet size measurement at room temperature (about 22–25 °C) was not conducted in our experiments.…”

“…Furthermore, Berton et al [ 15 ] reported that adsorbed proteins underwent a higher degree of structural modifications during the whole oxidation of β-lactoglobulin-stabilized O/W emulsions; nevertheless, unadsorbed proteins in the aqueous phase were much less prone to oxidized damage, which was clearly verified by unchanged protein solubility and no protein aggregation. Conversely, the results provided by intrinsic tryptophan fluorescence scanning in situ have suggested that decreased fluorescent intensity was a distinct consequence to indicate the structural modifications of the proteins induced by LPO during the storage of O/W emulsions [ 16 , 17 , 18 , 19 ]. Therefore, the protein position in O/W emulsions plays a crucial role in the evaluation of the protein modifications which are induced by LPO.…”

Effect of Oxidation on Quality of Chiba Tofu Produced by Soy Isolate Protein When Subjected to Storage

“…The carbonyl content in protein is reliable for oxidation because the protein carbonyls are formed as a result of oxidative modifications through the attack of ROS and its level indicates the extent of protein oxidation damage [ 21 ]. As present in Table 1 , the carbonyl content of SPI increased with storage time, which indicates that the degree of oxidative damage increased.…”

Effect of temperature of preheated soy protein isolate on the structure and properties of soy protein isolate heated–vitamin D 3 complex

“…The non‐covalent binding between SPI and vitamin D 3 (VD 3 ) is mainly through hydrophobic interaction (Chen et al., 2019). However, heat treatment of the protein will expose the hydrophobic group of the protein and promote the binding of small molecule compounds (Li et al, 2020). At present, there are no reports on the heat treatment of SPI and the delivery of VD 3 .…”