Although thermal treatments are beneficial for the preservation and safety of milk, they can also alter its immunogenic activity by affecting its protein components. To achieve precise results, it is essential to identify the specific proteins that cause food allergies. Therefore, investigating the possible alterations of cow\'s milk proteins (CMPs) resulting from thermal treatments is necessary. In this study, the Fourier transform infrared spectroscopy (FTIR) technique was used to analyze the effect of UHT thermal treatment on the secondary structures of milk casein. Using the second derivative, six characteristic peaks were identified in the Amide I region, ranging from 1700 to 1600 cm-1. It was found that thermal treatments produce shifts in absorption peaks, indicating changes in protein conformation and possibly in allergenic activity. These shifts were clearly identified in the first characteristic peak of samples M8 and M9, from 1621 to 1600 cm-1. The results suggest that thermal treatments may promote protein aggregation by increasing β turns and reducing β sheets and α helices, which could enhance the allergenic potential of the proteins and facilitate the formation of complexes between different milk proteins, such as β-lactoglobulin and κ-casein. Further studies are needed to experimentally validate the allergenic activity of proteins modified by thermal treatments, as only an analytical method (FTIR) was used to evaluate the secondary structures of the proteins.

(1) Background: Dietary protein is a key component of all dietary patterns. It has been demonstrated that there are subtle differences in health implications associated with the source of dietary protein consumed. This study examined dietary protein sources (DPSs) in a long-term study of diet-induced obesity ± ammonium hydroxide enhancement (AHE) and its role in improving long-term health outcomes. (2) Methods: Over 18 months, 272 C3H/HeJ mice (136 male and 136 female) were monitored on high-fat diets with varying DPSs ± AHE. Mice were monitored for weekly change in total mass, as well as 6-month assessments of lean and fat mass. At each assessment, a cohort (~8 mice per diet per sex) was censored for a cross-sectional examination of organ function. (3) Results: Longevity was improved in females fed AHE diets, regardless of DPSs. Females\' measures of fat and lean mass were markedly elevated with casein protein diets compared to beef protein diets regardless of AHE. Females fed a beef protein diet + AHE demonstrated reduced fat mass and increased lean mass with aging. In males, AHE beef protein diet-fed mice showed marked improvement to longevity and increased lean mass at 6 months. (4) Conclusions: This study demonstrates that dietary protein modification by AHE attenuates the negative impacts of HF diets in both males and females in a sex-dependent manner. Furthermore, the results from this study emphasize the importance of identifying the differences in the utilization of dietary proteins in both a sex- and age-related manner and demonstrate the potential of DPS modification by AHE as a dietary intervention.

The stability of diabetes formula food for special medical purposes (D-FSMP) was improved by high-pressure homogenization (HPH) at different homogenization pressures (up to 70 MPa) and number of passes (up to 6 times). The process at 60 MPa/4 times was the best. Casein had the highest surface hydrophobicity in this condition. The casein-polysaccharide complexes were endowed with the smallest size (transmission electron microscopy images). The complex particles exhibited nearly neutral wettability (the three-phase contact angle was 90.89°), lower interfacial tension, and the highest emulsifying activity index (EAI) and emulsifying stability index (ESI). The prepared D-FSMP system exhibited the narrowest particle size distribution range, the strongest interfacial deformation resistance and the best storage stability. Therefore, an appropriate intensity of HPH could enhance the stability of D-FSMP by improving the interfacial and emulsifying properties of casein-polysaccharide complexes. This study provides practical guidance on the productions of stable D-FSMP.

A hyperbranched poly (titanium oxide) (HBPTi) with hydroxyl terminal groups was synthesized via polycondensation reaction as a synergistic modifier with tannin to promote performance of casein-based composite film. The synergistic effects of HBPTis, acquiring different hyperbranched structures, with tannin on the microstructure, mechanical characteristics, barrier against water vapor, and thermal stability of casein-based film were investigated in this work. The tensile strength of the composite films increased from 7.6 MPa to 22.1 MPa, which accounts for 190.79 % increase after the addition of HBPTi compared to casein-tannin films modified with glycerol. The casein-tannin films with the help of HBPTi presented excellent water vapor permeation, thermal stability, and showed nearly 100 % UV absorption in the range 200-400 nm. Additionally, the microstructure of HBPTi modified casein-tannin films tend to be more compact due to the promoted interaction of casein-tannin composite aided by covalent bonding and/or other types of bonding between casein, tannin and HBPTi. Therefore, associative modification using such hyperbranched polymers and tannins provides extendable application value for casein-based films especially as food packaging materials and for other fields as well.

The global food system faces a challenge of sustainably producing enough food, and especially protein, to meet the needs of a growing global population. In developed countries, approximately 2/3 of protein comes from animal sources and 1/3 from plants. For an assortment of reasons, dietary recommendations call for populations in these countries to replace some of their animal protein with plant protein. Because it is difficult to substantially change dietary habits, increasing plant protein may require the creation of novel foods that meet the nutritional, orosensory, and functional attributes consumers desire. In contrast to plant-based milks, plant-based cheeses have not been widely embraced by consumers. The existing plant-based cheeses do not satisfactorily mimic dairy cheese as plant proteins are unable to replicate the functional properties of casein, which plays such a key role in cheese. One possible solution to overcome current constraints that is currently being explored, is to produce hybrid products containing soy protein and soybean-derived casein. Producing soybean-derived casein is possible by utilizing traditional genetic engineering tools, like Agrobacterium-mediated plant transformation, to express genes in soybeans that produce casein. If a cheese containing soy protein and soybean-derived casein satisfactorily mimics dairy, it presents an opportunity for increasing plant protein intake since US dairy cheese consumption has been steadily increasing. Soybeans are an excellent choice of crop for producing casein because soybeans are widely available and play a large role in the US and world food supply. Additionally, because a casein-producing soybean offers soybean farmers the opportunity to grow a value-added crop, expectations are that it will be welcomed by the agricultural community. Thus, there are benefits to both the consumer and farmer.

Tryptamine is a neuromodulator of the central nervous system. It is also a biogenic amine, formed by the microbial decarboxylation of L-tryptophan. Tryptamine accumulation in cheese has been scarcely examined. No studies are available regarding the factors that could influence its accumulation. Determining the tryptamine content and identifying the factors that influence its accumulation could help in the design of functional tryptamine-enriched cheeses without potentially toxic concentrations being reached. We report the tryptamine concentration of 300 cheese samples representing 201 varieties. 16% of the samples accumulated tryptamine, at between 3.20 mg kg-1 and 3012.14 mg kg-1 (mean of 29.21 mg kg-1). 4.7% of cheeses accumulated tryptamine at higher levels than those described as potentially toxic. Moreover, three technological/metabolic/environmental profiles associated with tryptamine-containing cheese were identified, as well as the hallmark varieties reflecting each. Such knowledge could be useful for the dairy industry to control the tryptamine content of their products.

The influence of Carboxymethyl chitosan (CMCS) on the emulsification stability mechanism of casein (CN) and its effects on the stability of whole nutrient emulsions were investigated. The complex solutions of CN and CMCS were prepared and the turbidity, ultraviolet (UV) absorption spectrum, fluorescence spectrum, circular dichroism (CD) spectrum, Fourier transform infrared (FTIR) spectrum, interfacial tension and microstructural observations were used to study the inter-molecular interaction of CMCS and CN. The effects of CMCS on the emulsion stability of CN were further analyzed by particle size, ζ-potential, instability index and rheological properties. Moreover, the accelerated stability of whole nutrient emulsions prepared by CMCS and CN was evaluated. The results revealed that CN-CMCS complexes were mainly formed by hydrogen bonding. The stability of the CN-CMCS composite emulsions were improved, as evidenced by the interfacial tension decreasing from 165.96 mN/m to 158.49 mN/m, the particle size decreasing from 45.85 μm to 12.98 μm, and the absolute value of the potential increasing from 29.8 mV to 33.5 mV. The stability of whole nutrient emulsion was also significantly enhanced by the addition of CN-CMCS complexes. Therefore, CN-CMCS complex could be served as a novel emulsifier to improve the stability of O/W emulsions.

Exosomes are cell-derived extracellular vesicles (EVs) with diameters between 30 and 120 nm. In recent years, several studies have evaluated the therapeutic potential of exosomes derived from different fluids due to their low immunogenicity and high biocompatibility. However, producing exosomes on a large scale is still challenging. One of the fluids from which they could be isolated in large quantities is milk. Moreover, regeneration is a well-known property of milk. The present work seeks to optimize a method for isolating exosomes from bovine and human milk, comparing different storage conditions and different extraction protocols. We found differences in the yield extraction associated with pre-storage milk conditions and observed some differences according to the processing agent. When we removed milk fat globules and added rennet before freezing, we obtained a cleaner final fraction. In summary, we attempted to optimize a rennet-based new milk-exosome isolation method and concluded that pre-treatment, followed by freezing of samples, yielded the best exosome population.

In the present study, different oligosaccharides (fructooligosaccharide (FOS), galactooligosaccharide (GOS), isomaltooligosaccharide (IMO), and xylooligosaccharide (XOS)) were modified on casein (CN) via Maillard reaction. The CN-oligosaccharide conjugates were evaluated for modifications to functional groups, fluorescence intensity, water- and oil-holding properties, emulsion foaming properties, as well as general emulsion properties and stability. The results demonstrated that the covalent combination of CN and oligosaccharides augmented the spatial repulsion and altered the hydrophobic milieu of proteins, which resulted in a diminution in water-holding capacity, an augmentation in oil-holding capacity, and an enhancement in the emulsification properties of proteins. Among them, CN-XOS exhibited the most pronounced changes, with the emulsification activity index and emulsion stability index increasing by approximately 72% and 84.3%, respectively. Furthermore, CN-XOS emulsions have smaller droplet sizes and higher absolute potential values than CN emulsions. Additionally, CN-XOS emulsions demonstrate remarkable stability when ion concentration and pH are varied. These findings indicate that oligosaccharides modified via Maillard reaction can be used as good natural emulsifiers. This provides a theoretical basis for using oligosaccharides to modify proteins and act as natural emulsifiers.

High-pressure processing (HPP) is a promising alternative to thermal pasteurization. Recent studies highlighted the effectivity of HPP (400-600 MPa and exposure times of 1-5 min) in reducing pathogenic microflora for up to 5 logs. Analysis of modern scientific sources has shown that pressure affects the main components of milk including fat globules, lactose, casein micelles. The behavior of whey proteins under HPP is very important for milk and dairy products. HPP can cause significant changes in the quaternary (> 150 MPa) and tertiary (> 200 MPa) protein structures. At pressures > 400 MPa, they dissolve in the following order: αs2-casein, αs1-casein, k-casein, and β-casein. A similar trend is observed in the processing of whey proteins. HPP can affect the rate of milk fat adhering as cream with increased results at 100-250 MPa with time dependency while decreasing up to 70% at 400-600 MPa. Some studies indicated the lactose influencing casein on HP, with 10% lactose addition in case in suspension before exposing it to 400 MPa for 40 min prevents the formation of large casein micelles. Number of researches has shown that moderate pressures (up to 400 MPa) and mild heating can activate or stabilize milk enzymes. Pressures of 350-400 MPa for 100 min can boost the activity of milk enzymes by up to 140%. This comprehensive and critical review will benefit scientific researchers and industrial experts in the field of HPP treatment of milk and its effect on milk components.
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