98%
921
2 minutes
20
Glycomacropeptide (GMP) shows potential for enhancing the rehydration properties of high-protein dairy powders due to its hydrophilic nature. This study involved formulating micellar casein concentrate (MCC) solutions (8.6% final protein content) with 0, 10, and 20% GMP as a percentage of total protein, and investigated the physicochemical and rehydration properties of the resultant freeze-dried powders (P-MCC-0G, P-MCC-10G, and P-MCC-20G, respectively). The surface charges of caseins in the control MCC and 10 or 20% GMP blended solutions were -25.8, -29.6, and -31.5 mV, respectively. Tablets prepared from P-MCC-10G or P-MCC-20G powders displayed enhanced wettability with contact angle values of 80.6° and 79.5°, respectively, compared with 85.5° for P-MCC-0G. Moreover, blending of GMP with MCC resulted in faster disintegration of powder particles during rehydration (i.e., dispersibility) compared to P-MCC-0G. Faster and more extensive release of caseins from powder particles into solution was evident with the increasing proportion of GMP, with the majority of GMP released within the first 15 min of rehydration. The results of this study will contribute to further development of formulation science for achieving enhanced solubility characteristics of high-protein dairy powder ingredients, such as MCC.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8394547 | PMC |
http://dx.doi.org/10.3390/foods10081960 | 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).
View Article and Find Full Text PDF