Bovine milk contains four types of caseins with β-casein being one of the most abundant. Previous studies on cow milk have reported seemingly contradictory effects of β-casein on milk renneting behavior. The aim of this study was to gain a better understanding of how β-casein affects the properties and renneting behavior of casein micelles by using a model system of reassembled casein micelles (RCMs). We increased the β-casein ratio of RCMs to 60 % by adjusting the β-casein ratio during or after the reassembly process. We found that reducing the calcium phosphate content to 85 % was necessary for forming stable β-casein enriched RCMs. It was also found that adding β-casein during reassembly resulted in firmer rennet coagulates compared to adding it afterwards. To conclude, the order of adding β-casein significantly affected the structure formation and, consequently, the properties of RCMs.
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http://dx.doi.org/10.1016/j.foodchem.2025.142951 | DOI Listing |
Food Chem
January 2025
Food Quality & Design Group, Wageningen University and Research, 6708, WG, Wageningen, The Netherlands.
Bovine milk contains four types of caseins with β-casein being one of the most abundant. Previous studies on cow milk have reported seemingly contradictory effects of β-casein on milk renneting behavior. The aim of this study was to gain a better understanding of how β-casein affects the properties and renneting behavior of casein micelles by using a model system of reassembled casein micelles (RCMs).
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Food and Nutrition, Joint Research Center for Food Nutrition and Health of IHM, Anhui Agriculture University, Hefei, Anhui 230036, China. Electronic address:
Micelle systems using safe food-grade biopolymers are of particular interest for the encapsulation and delivery of nutrition components. Micellar casein (MC) was assembled using transglutaminase (TGase) to couple with phosphoserine peptide, which enhance the stability of docosahexaenoic acid (DHA) from algae oil. The mechanism behind the construction of MC-phosphoserine peptide and the encapsulation of DHA was explored.
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 PDFFoods
January 2025
A.N. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, 28 ul. Vavilova, Moscow 119991, Russia.
The hydrolysis of proteins by proteases (proteolysis) plays a significant role in biology and food science. Despite the importance of proteolysis, a universal quantitative model of this phenomenon has not yet been created. This review considers approaches to modeling proteolysis in a batch reactor that take into account differences in the hydrolysis of the individual peptide bonds, as well as the limited accessibility (masking) for the enzymes of some hydrolysis sites in the protein substrate.
View Article and Find Full Text PDFFood Res Int
January 2025
Institut Numecan, INSERM, INRAE, Univ Rennes, Rennes, France. Electronic address:
Dietary protein reduces energy intake in following meals by signaling directly or indirectly to the brain. We recently observed differences in plasma amino acid kinetics and intra-gastric behavior between micellar casein (MC) and sodium caseinate (SC) in pigs, two factors that impact food intake. Our objective was to clarify whether the supramolecular structure of casein, given as a preload to pigs, impacts on subsequent food intake.
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