Background: Whey protein supplements might be a potential risk factor for the restoration surface due to its pH and lactose content.
Aim: The study aimed to evaluate the effect of whey protein beverages on the microhardness of four restorative composites with different microstructures (Filtek Z 350XT, Filtek Z 250XT, Filtek Bulk Fill (FBF), and Filtek 60).
Materials And Methodology: Forty disc-shaped samples from each material (in total 160) were prepared and wet polished. The samples of each group were randomly divided into four subgroups and subjected to four immersion media namely, whey protein Concentrate (WPC), whey protein Isolate (WPI), whey protein water (WPW), and distilled water (DW). The immersion protocol was performed twice for 10 min daily for 30 days followed by immersion in artificial saliva for another 10 min and stored in DW till the next cycle. The pre immersion and post immersion microhardness of all the samples were recorded with a Microhardness Tester FM-800. Data obtained were statistically analyzed using SPSS 25 software.
Results And Conclusions: All composites exhibited decline in microhardness, except for FBF. 60 composites which showed the highest decline in microhardness. WPC and WPI caused the greatest reduction in microhardness compared to WPW.
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http://dx.doi.org/10.4103/Jcd.Jcd_140_21 | DOI Listing |
Food Chem
January 2025
Department of Food Science and Technology, Faculty of Agriculture, Ferdowsi University of Mashhad, Azadi Sq., Mashhad, Khorasan Razavi P.O. Box 9177948944, Iran. Electronic address:
Protein fibrillation complex mechanisms led to an emerging trend in research for years. The mechanisms behind whey protein isolate (WPI) fibrillation driven by divalent cations remained still a matter of speculation. All cations (Ca, Fe, Mg, and Zn) enhanced the microenvironment polarity through π-π stacking, and the amide I and II shifts confirmed the fibrillation.
View Article and Find Full Text PDFFood Chem
January 2025
Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, College of Food Science, Southwest University, Chongqing 400715, China,. Electronic address:
Baked milk is subjected to prolonged high-temperature processing, which often undermines its dispersion stability. While carrageenan is known to inhibit milk demixing, its role in stabilizing heat-induced protein aggregates remains inadequately understood. In this study, we isolated casein micelles (CM), whey protein-casein aggregates (WPCA), and whey protein aggregates (WPA) from baked milk through centrifugation.
View Article and Find Full Text PDFVet Res Commun
January 2025
Pollution Laboratory, Freshwater and Lakes Division, National Institute of Oceanography and Fisheries (NIOF), Cairo, Egypt.
This investigation looked at the ameliorative role of camel whey protein hydrolysates-diet (PH) in Oreochromis niloticus stocked under alkaline conditions. One hundred sixty fish (16.02 ± 0.
View Article and Find Full Text PDFInt 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.
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