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http://dx.doi.org/10.1385/1-59259-183-3:097 | DOI Listing |
Microorganisms
January 2025
Institute of Food Science and Biotechnology, Department of Bioprocess Engineering, University of Hohenheim, Fruwirthstraße 12, 70599 Stuttgart, Germany.
Background: Cow's milk represents an important protein source. Here, especially casein proteins are important components, which might be a promising source of alternative protein production by microbial expression systems. Nevertheless, caseins are difficult-to-produce proteins, making heterologous production challenging.
View Article and Find Full Text PDFAnimals (Basel)
January 2025
College of Animal Science and Technology, Henan Agricultural University, Zhengzhou 450046, China.
Reportedly, the number of κ-casein (κ-CN) B alleles increases the proportion of κ-CN to total protein and the κ-CN content. This phenomenon is caused by single-nucleotide polymorphisms (SNPs) in the promoter region of , which encodes the B variant. Therefore, a series of 5'-deleted promoter plasmids were constructed to define the core promoter of .
View Article and Find Full Text PDFFoods
January 2025
Food Studies and Policies Section, Food Safety Department, Dubai Municipality, Dubai P.O. Box 330127, United Arab Emirates.
High-pressure processing (HPP) is used as a non-thermal approach for controlling microbial viability. The purposes of this study were to (i) establish the decimal reduction times (D-values) for pathogenic bacteria during 350 MPa HPP treatment,; (ii) evaluate the impact of 350 MPa HPP on total plate count (TPC), yeasts and molds (YM), and lactic acid bacteria (LAB) in camel milk; (iii) investigate the behavior of several spoilage-causing bacteria during storage at 4 °C and 10 °C for up to 10 d post-HPP treatment; and (iv) assess the effect of HPP on the protein degradation of camel milk. The D-values for , O157:H7, and spp.
View Article and Find Full Text PDFFood Res Int
February 2025
College of Food Science, Southwest University, Chongqing 400715, PR China. Electronic address:
This study applied high hydrostatic pressure (HHP) treatment to buffalo milk casein to assess the influence of different pressure levels on its structural characteristics, physicochemical properties, and functional properties. The results showed that although HHP had no marked impact on the zeta potential and secondary structure, it altered the protein's spatial structure (primarily its tertiary structure), and improved dispersion properties (such as particle size, solubility, and turbidity), as well as foaming properties. Additionally, HHP improved the antioxidant activity and antibacterial activity against Escherichia coli.
View Article and Find Full Text PDFFood Res Int
February 2025
Department of Agriculture, University of Naples "Federico II", 80055 Portici, Italy.
β-Casomorphins (BCMs), food-associated peptides resulting from the proteolytic cleavage of β-casein (β-CN), have been widely investigated for their opioid-like activity. This research aimed to identify the presence of BCM7, BCM6, and BCM5 in different bovine milk-deriving blue cheese types and to describe the intricate mechanisms behind their formation, focusing on their origin from cheese with β-CN A1 and A2 variants. Using nanoLC-ESI-Q-Orbitrap-MS/MS and advanced computational tools, we explored the peptidomes of Bleu d'Auvergne, Gorgonzola, Stilton, and Bergader blue cheeses from milk containing both β-CN A1 and A2 variants.
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