This study investigated structural changes and the in vivo retention in the oral cavity of heated whey protein concentrate (WPC). Heated WPC was shown to have both a higher retention time in the oral cavity compared to unheated whey protein up to 1 min post swallow, and a concomitant increase in free thiol concentration. Nuclear magnetic resonance and circular dichroism demonstrated structural changes in the secondary and tertiary structures of the WPC upon heating. Structural loss of the β-barrel was shown to increase during heating, leading to the exposure of hydrophobic regions. The increase in free thiols and hydrophobic regions are two factors which are known to increase mucoadhesive strength and hence increase oral retention of heated whey protein which may subsequently increase the perception of mouthdrying.
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http://dx.doi.org/10.1016/j.foodchem.2021.131650 | DOI Listing |
Int J Biol Macromol
January 2025
School of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China; Engineering Research Center of Grain Deep-processing and High-efficiency Utilization of Jilin Province, Changchun 130118, China. Electronic address:
Emulsions play an important role in food systems by encapsulating and delivering active compounds, but maintaining their stability under various conditions can be challenging. This study explored how the concentrations of Tremella polysaccharides (TPs) (0-0.75 %) affects the structural of whey protein isolate (WPI) and the stability of their emulsions at pH 4.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Department of Engineering Mechanics, KTH Royal Institute of Technology, 100 44 Stockholm, Sweden.
We here explore confinement-induced assembly of whey protein nanofibrils (PNFs) into microscale fibers using microfocused synchrotron X-ray scattering. Solvent evaporation aligns the PNFs into anisotropic fibers, and the process is followed in situ by scattering experiments within a droplet of PNF dispersion. We find an optimal temperature at which the order parameter of the protein fiber is maximized, suggesting that the degree of order results from a balance between the time scales of the forced alignment and the rotational diffusion of the fibrils.
View Article and Find Full Text PDFFood Chem X
January 2025
Key Laboratory of Dairy Science, Ministry of Education, Food Science College, Northeast Agricultural University, Harbin, 150030, China.
Whey proteins, the most abundant proteins in human milk (HM), play a vital role in the growth and development of infants. This review first elaborates on the main components of HM whey proteins, including various proteins with specific functions, and details the functions of these proteins in terms of infant nutrition, immunity, as well as growth and development. Secondly, it analyzes factors that affect HM whey proteins, such as maternal differences, dietary habits, and geographical differences.
View Article and Find Full Text PDFFood Funct
January 2025
School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
Lactopontin (LPN) is an important milk protein with the potential to improve bone health; however, its specific effects have not been determined. This study aims to investigate the effects of LPN on early bone growth and development. 3 week-old SD rats ( = 32) were assigned to the control group, whey protein concentration (WPC) group, LPN-L (low-dose LPN) group, and LPN-H (high-dose LPN) group, with intragastric administration of deionized water, 65.
View Article and Find Full Text PDFThe aim of this study was to use blue whiting fish protein hydrolysate (BWFPH) as a novel dietary amino acid supplement in whey protein isolate (WPI) and pea protein isolate (PPI)-based protein bars. The findings indicate that incorporating BWFPH significantly influenced the nutritional profile of the protein bars, leading to a ~93% reduction in hardness compared to bars without the hydrolysate. Additionally, BWFPH effectively delayed the hardening process during storage.
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