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Micellar casein (MC) has a unique gastric colloidal behavior in response to Ca cross-linking, and its aggregation properties are closely related to pepsin and gastric acid. In this study, MC with different levels of colloidal calcium phosphate (CCP) was obtained by high hydrostatic pressure (HHP) at different pressures, followed by spray drying to obtain the powders. Different amounts of calcium chloride (exogenous Ca) were added to MC powders prior to in vitro simulated digestion to investigate the effect of exogenous serum Ca levels on the aggregation behavior and the structure change of curds generated in gastric tract. The results revealed that HHP induced the emergence of more Ca-binding sites, thus Ca was more likely to bind to MC matrix with low CCP levels. Meanwhile, high serum Ca level provided more opportunities to form aggregates. The Highest pressure (500 MPa) with the highest Ca level (5 mM) caused the lowest solubility aggregates, which were only 30% at the end of gastric digestion (120 min), half of the control sample (0 MPa with 0.15 mM Ca). The results of wide-angle X-ray scattering / small-angle X-ray scattering suggested that both pepsin and gastric acid-induced aggregation via Ca as a bridge. For pepsin, Ca cross-linked between para-κ-casein; For gastric acid, Ca recombined phosphorylation sites and caused cross-linking of casein subunits.
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http://dx.doi.org/10.1016/j.foodres.2023.113558 | DOI Listing |
Nutrients
August 2025
Birmingham Children's Hospital, NHS Trust, Steelhouse Lane, Birmingham B4 6NH, UK.
: The rate at which amino acids (AAs) are absorbed from casein glycomacropeptide (CGMP) when given as a protein substitute in phenylketonuria (PKU) is unknown. This three-way randomised, controlled, crossover study aimed to compare the AA absorption profile of phenylalanine (Phe)-free L-amino acids (L-AAs), low-Phe CGMP (CGMP) and casein in healthy adult subjects. : Area under the curve (AUC) was measured over 240 minutes after ingesting one dose of each protein source on three separate occasions, under the same test conditions.
View Article and Find Full Text PDFFoods
July 2025
Associate Professorship of Food Process Engineering, Department of Life Science Engineering, TUM School of Life Sciences, Technical University Munich, 85354 Freising, Germany.
The covalent cross-linking of caseins by the enzyme transglutaminase (Tgase) stabilizes the structure of casein micelles. In our study, the effects of a pretreatment of skim milk (SM) by Tgase on milk protein fractionation by microfiltration were tested. Tgase was found to induce amount-dependent modifications of all milk proteins in SM and a reduction in deposit resistance for laboratory dead-end filtrations of up to 20%.
View Article and Find Full Text PDFJ Nutr Sci
July 2025
Center for Translational Medicine, Semmelweis University, Üllői út 26, 1085 Budapest, Hungary.
Amateur and professional athletes often consume protein supplements to accelerate muscle gain; however, it has been suggested that these products not only are associated with risks when consumed excessively. Several recent reports have indicated that certain products are contaminated with heavy metals. Therefore, in this study, we aimed to investigate protein powders in Hungary for heavy metal contamination.
View Article and Find Full Text PDFBiomacromolecules
August 2025
Department of Chemistry, Indian Institute of Technology Hyderabad, Kandi, Sangareddy, Telangana 502284, India.
Herein, we unveil the interaction between bilirubin (BIL), a liver metabolite, and a milk protein, casein (CAS), through an integrated experimental-computational approach. Encapsulation of BIL within CAS protein micelles was characterized by using UV-vis absorption, steady-state fluorescence, and circular dichroism (CD) spectroscopy. CD analysis revealed conformational modulation of BIL upon encapsulation, accompanied by Förster resonance energy transfer (FRET) from CAS's tryptophans to BIL.
View Article and Find Full Text PDFInt J Mol Sci
June 2025
Chair of Soft Matter Process Engineering (AVT.SMP), RWTH Aachen University, 52074 Aachen, Germany.
This study systematically investigates how thiol-disulfide interactions influence the structure and mechanical properties of casein gels. Acid gels were prepared from suspensions of micellar casein (MC) powder that were heat-treated at 70 °C. Thiol groups were variably blocked with N-ethylmaleimide (NEM).
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