Search Results (1,333)

Bovine colostrum (BC), the first milk secreted by mammals after birth, is a trending alternative source for supplementing infants and children, offering benefits for gut and immune health. Its rich components, such as proteins, immunoglobulins, lactoferrin, and glycans, are used to fortify diets and support development. Preterm development is crucial, especially in the maturation of essential systems, and from 2010 to 2020, approximately 15% of all premature births occurred at less than 32 weeks of gestation worldwide. This review explores the composition, benefits, and effects of BC on general infants and children, along with preterm infants who require special care, and highlights its role in growth and development. BC is also associated with specific pediatric diseases, including necrotizing enterocolitis (NEC), infectious diarrhea, inflammatory bowel disease (IBD), short-bowel syndrome (SBS), neonatal sepsis, gastrointestinal and respiratory infections, and some minor conditions. This review also discusses the clinical trials regarding these specific conditions which are occasionally encountered in preterm infants. The anti-inflammatory, antimicrobial, immunomodulatory, and antiviral properties of BC are discussed, emphasizing its mechanisms of action. Clinical trials, particularly in humans, provide evidence supporting the inclusion of BC in formulas and diets, although precise standards for age, feeding time, and amounts are needed to ensure safety and efficacy. However, potential adverse effects, such as allergic reactions to caseins and immunoglobulin E, must be considered. More comprehensive clinical trials are necessary to expand the evidence on BC in infant feeding, and glycans, important components of BC, should be further studied for their synergistic effects on pediatric diseases. Ultimately, BC shows promise for pediatric health and should be incorporated into nutritional supplements with caution. Full article

Background/Objectives: Melanoma malignum is considered the most dangerous form of skin cancer, characterized by the exceptional resistance to many conventional chemotherapies. The aim of this study was to evaluate the effect of Nutramil^TM Complex (NC)—Food for Special Medical Purpose (FSMP), on two types of melanoma cell lines, primary WM115 and malignant WM266-4. Methods: At 24 h after seeding, growth medium was replaced with a medium containing encoded treatments of NC or NC-CC (Nutramil^TM Complex without calcium caseinate) at various concentrations. Cells were treated for 24, 48, and 72 h. Results: Our results showed that Nutramil^TM Complex reduces proliferation of malignant melanoma WM266-4 cells but did not affect the proliferation of WM115 primary melanoma. This was followed by measured down-regulation of selected pro-survival proteins expression in WM266-4 cells, specifically ERK1/2, AKT-1, HSP27, Survivin, and TAK1. Interestingly, our results showed elevated levels of some pro-apoptotic proteins in both cell lines, including Bad, Smad2, p38MAPK, cleaved forms of Caspase-3/7, as well as cleaved PARP. Conclusions: Taken together, our results indicate that various melanoma cancer cell lines may respond in a different way to the same compound. They also suggest induction of apoptotic pathway by Nutramil^TM Complex as the most likely mechanism of its anticarcinogenic activity. Full article

This study aimed to evaluate the change in enamel color and surface micro-hardness following the use of resin-infiltration concept material (ICON) and casein phosphopeptide-amorphous calcium fluoride phosphate (CPP-ACFP) remineralizing agent. Fifty-four extracted human third molars were collected and randomly divided into three groups: group A: control with no surface treatment; group B: treated using ICON; and group C: treated using CPP-ACFP. The change in color and micro-hardness of the enamel surface were measured using spectrophotometer and Vickers hardness number, respectively. The measurements were taken at three timelines; baseline (BL), after demineralization (DM), and after surface treatment (TX). The three groups showed no significant differences in enamel color change after demineralization (p < 0.05). However, after surface treatment in relation to the baseline, groups B and C had a significant increase in color change compared to the control group (p < 0.05), and group B showed a statistically significant increase in enamel color changes compared to group C. Additionally, all groups exhibited a significant reduction in enamel micro-hardness after demineralization in comparison to their baseline (p < 0.05). Group C showed a significant increase in micro-hardness after surface treatment compared to groups A and B (p < 0.05), while group B showed a significant decrease in enamel micro-hardness compared to groups A and C (p < 0.05). These findings suggest that teeth treated with CPP-amorphous calcium fluoride phosphate (CPP-ACFP) show a significant improvement in enamel surface color after demineralization compared to the teeth treated with resin infiltration (ICON) and the non-treated teeth. Additionally, enamel surfaces treated with CPP-ACFP show significant enamel hardness regaining, while resin infiltration (ICON) compromises enamel surface hardness. Full article

Alzheimer’s disease (AD), a leading neurodegenerative disorder, is closely associated with the accumulation of amyloid-beta (Aβ) peptides in the brain. The enzyme β-secretase (BACE1), pivotal in Aβ production, represents a promising therapeutic target for AD. While bioactive peptides derived from food protein hydrolysates have neuroprotective properties, their inhibitory effects on BACE1 remain largely unexplored. In this study, we evaluated the inhibitory potential of protein hydrolysates from gliadin, whey, and casein proteins prepared using bromelain, papain, and thermolysin. Through in vitro and cellular assays, bromelain-hydrolyzed gliadin (G-Bro) emerged as the most potent BACE1 inhibitor, with an IC₅₀ of 0.408 mg/mL. G-Bro significantly reduced BACE1 expression and amyloid precursor protein (APP) processing in N2a/PS/APP cell cultures, suggesting its potential to attenuate Aβ aggregation. The unique peptide profile of G-Bro likely contributes to its inhibitory effect, with proline residues disrupting β-sheets, lysine residues introducing positive charges that hinder aggregation, hydrophobic residues stabilizing binding interactions, and glutamine residues enhancing solubility and stability. These findings highlight gliadin hydrolysates, particularly G-Bro, as potential natural BACE1 inhibitors with applications in dietary interventions for AD prevention. However, further studies are warranted to elucidate specific peptide interactions and their bioactivity in neural pathways to better understand their therapeutic potential. Full article

In this study, two methods for assessing the purity of A2 fermented milk and β-casein genotypes in dairy cows were examined. The need for rapid and precise methods for herd screening and A2 milk quality control justified this study. Accordingly, an ELISA test was developed to identify β-casein A1 in fermented milk, and a commercial Lateral Flow Immunoassay (LFIA) was evaluated to determine A2A2 genotypes and the purity of A2 milk. The results demonstrated 100% sensitivity and specificity of the ELISA test in identifying β-casein A1. The LFIA test successfully identified A2A2 genotypes and confirmed the purity of A2 milk, with a minimum detectable contamination of 5% for raw milk and 10% for fermented milk. Both tests exhibited 100% sensitivity and specificity, resulting in positive and negative predictive values of 100%. The positive likelihood ratio was infinite, while the negative was zero, indicating a precise and reliable test with no false diagnoses. Compared to traditional genotyping, these methods proved to be more practical and showed potential for large-scale screening. It was concluded that ELISA and LFIA are valuable tools for ensuring the quality and authenticity of A2 milk, meeting the demands of producers and consumers for safe and healthy dairy products. Full article

Phenylalanine (Phe) is a potentially limiting amino acid for lactating cows. The mechanism by which Phe regulates milk protein synthesis remains unclear. The present study elucidates the mechanisms by which phenylalanine affects milk protein synthesis, amino acid utilization, and related signaling pathways in bovine mammary epithelial cells (BMECs). The BMECs were treated with five concentrations (0, 0.22, 0.44, 0.88, 1.76 mM, and serum free). Rapamycin inhibitors and RNA interference (RNAi) were used to inhibit the phosphorylation of the mammalian target of rapamycin (mTOR) signaling pathway and the expression of relevant amino acid transporters, respectively. The results showed that 4×Phe (0.88 mM) significantly increased (p < 0.05) both the mRNA and protein expression of α-casein (CSN1S1), β-casein (CSN2), and κ-casein (CSN3), as well as L-type amino acid transporter-1 (LAT1) mRNA expression. Protein expression and modification assays of mTOR-related proteins showed that 4×Phe could increase (p < 0.05) the expression of α-casein and eukaryotic initiation factor 4E-binding protein-1 (4EBP1) and tended to increase the expression of ribosomal protein S6 protein kinase (S6K1, p = 0.054). The general control nonderepressible 2 (GCN2) signaling pathway factor, eukaryotic initiation factor 2 (eIF2α), was downregulated by 4×Phe treatment (p < 0.05). The rapamycin inhibition test showed that Phe regulated casein synthesis via the mTOR signaling pathway. RNAi experiments showed that LAT1 mediated the entry of Phe into cells. Moreover, 4×Phe treatment tended to decrease (0.05 < p < 0.10) the consumption of valine, leucine, histidine, tyrosine, cysteine, alanine, asparagine, and serine in the medium. Collectively, phenylalanine enhanced α-casein synthesis by regulating the phosphorylation of 4EBP1 and eIF2α and promoting the formation of the mTOR-centered casein translation initiation complex. Full article

This review aims to compile and present information on polycyclic aromatic hydrocarbons (PAHs) in milk, their effects on human health, relevant legal regulations, and methods for their detection. PAHs are hazardous environmental pollutants that can accumulate in milk due to their lipophilicity and feed, water, and grass contamination. Also, high-temperature processing in the milk industry can contribute to their formation. PAHs are recognized for their carcinogenic, mutagenic, and teratogenic properties, posing significant risks to human health. Milk presents a unique analytical challenge as a complex matrix; the fats where hydrophobic PAHs tend to accumulate are “trapped” within the membranes of casein micelles. This complexity makes the extraction and analysis of PAHs more demanding than other food matrices. Developments in chromatographic techniques provide effective methods for detecting PAHs in milk, ensuring adherence to regulatory standards. The proper planning of research and the use of these techniques will lead to accurate results. This review focuses specifically on methods for extracting and isolating PAHs from milk, and instrumental methods for their detection and quantification. Such a review may be valuable for researchers looking for methods to analyze PAHs in milk and dairy products. Full article

Blood waste originating from slaughterhouse activities in China is considered to be massive, and improper handling may cause epidemic diseases and environmental pollution. This research aimed to obtain a potential bacterial strain for blood protein degradation by isolating indigenous bacteria from slaughterhouses. Isolation was carried out by using dilution plate coating, while blood agar and casein plates were used to screen potential strains. Morphological, physiological, and biochemical characterizations, as well as 16S rRNA sequencing, were performed to identify the selected strain. The optimization of enzyme production was performed by using the Plackett–Burman test and response surface methodology. A strain coded NwMCC01910137 was isolated and screened to effectively degrade bovine blood protein and was identified as Bacillus subtilis. The optimum culture conditions for enzyme production included a fermentation temperature of 37.4 °C, an initial pH of 7.7, a soybean meal powder addition amount of 3.00% (w/v), a glucose level of 3.8% (w/v), a NaCl level of 0.3 g/L, a phosphate concentration of 2.5 g/L, an inoculum size of 2.5 g/L (4%), and a fermentation time of 48 h. Under the optimum condition, the strain showed enzyme activity of 166.83 U/mL. Hence, the isolated B. subtilis showed good activity in bovine blood protein degradation and has good application potential for slaughterhouse waste processing. Full article

Angiotensin-converting enzyme (ACE) inhibitory peptides exhibit antihypertensive effects by inhibiting ACE activity, and the study of the interaction between ACEs and inhibitory peptides is important for exploring new therapeutic strategies. In this study, the ACE-inhibitory peptide isolated from casein hydrolysate with the amino acid sequence Leu–Leu–Tyr (LLY) exhibited high ACE-inhibitory activity and stability, which holds significant implications for biochemistry and pharmaceutical applications. Furthermore, systematic investigations were conducted on the interaction between ACE and LLY through various approaches. The Lineweaver–Burk plot indicated the non-competitive inhibition pattern of LLY, suggesting that it binds to the enzyme at the non-active site, and the results were further validated by a molecular docking study. Additionally, multispectral experiments and atomic force microscopy were conducted to further elucidate the underlying mechanism of peptide activity. The findings indicated that LLY could induce a conformational change in ACE, thereby inhibiting its activity. This study contributes to a deeper understanding of the mechanism of action of ACE-inhibitory peptides and bears important significance for drug development in hypertension. Full article

The amino acid (AA) content of multiple samples of various dairy powders was determined, providing a comprehensive evaluation of the differences in AA profiles attributable to distinct manufacturing processes. Products examined included whole milk powder (WMP), skim milk powder (SMP), cheese whey protein concentrate (WPC-C), lactic acid casein whey protein concentrate (WPC-L), high-fat whey protein concentrate (WPC-HF), hydrolyzed whey protein concentrate (WPH), whey protein isolate (WPI), and demineralized whey protein (D90). WMP and SMP exhibited broadly similar AA profiles, with minor differences likely due to the minimal milk fat protein content, which is nearly absent from SMP. Comparative analysis of WPC-C and WPC-L indicated higher levels of threonine, serine, glutamic acid, and proline in WPC-C but lower levels of tyrosine, phenylalanine, and tryptophan, attributed to the different methods of separation from casein proteins. WPI and WPC-HF originate from similar sweet whey streams but follow divergent processing methods; consequent on this were variations in the levels of all AAs except histidine. The nanofiltration step in D90 production retains its non-protein nitrogen content and affects its AA profile; consequently, D90 consistently exhibited lower AA levels than WPC-C. These findings underscore the significant impact of manufacturing processes on dairy powder AA composition. Full article

Caseinate is commonly used in the dairy industry for its stabilizing properties. Its functionalities are largely due to its manufacturing process involving a high level of demineralization that induces casein precipitation. To address this, the researchers are looking for alternatives to respond to consumer demands for high-quality ingredients and increase efficiency. In the present study, we explored low demineralization (0–43%) that preserves the casein integrity to produce caseins that can substitute caseinate in whipping creams (WC). The physicochemical, structural, and functional properties of these caseins were evaluated to assess their viability as surface-active agents in blend-fat whipping cream. The results showed that a demineralization level over 43% significantly impacts the size, secondary structures (β-sheets, β-turns, and α-helices particularly), and surface hydrophobicity that favorably impact the emulsifying properties but diminish the foam stability. WC made with caseins demineralized at 0 and 13% provided stable foam, with the lowest emulsion stability at 0% of demineralization. Using demineralized caseins at 13% offers a sustainable alternative to caseinate in food products requiring stable foams as WCs without significantly altering other desired functionalities such as overrun and emulsion stability. Further research studies into optimizing the demineralization process and exploring applications in other food matrices are suggested. Full article

A plant-based diet is considered a promising approach for managing hyperuricemia (HUA). This study examined the effects of soy protein and plant-based oils on HUA-induced inflammation and immune dysfunction. Male Wistar rats, induced with HUA using oxonic acid and uric acid (UA), were fed casein or soy protein with palm or safflower oil (2 × 2 factorial design) for 8 weeks. HUA rats had lower serum albumin and T cell percentages in peripheral blood leukocytes (PBLs) and splenocytes, along with increased leukocyte counts and spleen weights, compared to healthy rats (p < 0.05). Soy protein improved HUA-induced reductions in albumin, while safflower-seed oil ameliorated reductions in albumin, plasma interleukin (IL)-4, and T-suppressor splenocytes, and mitigated elevated serum UA, plasma IL-6, and B leukocytes (two-way ANOVA, p < 0.05). In PBL, soy protein alleviated HUA-induced decreases in TNF-α, casein and palm oil increased IL-6, and casein further reduced IFN-γ production. Under Con A stimulation, casein and safflower-seed oil alleviated decreases in IL-6 and IL-10, respectively, while under LPS stimulation, casein further increased TNF-α production. In splenocytes, soy protein and safflower-seed oil reduced HUA-induced increases in TNF-α and increased IL-10, and safflower-seed oil increased IL-6 production. Under Con A stimulation, soy protein and safflower-seed oil reduced TNF-α and increased IL-10 production in splenocytes. The findings suggest that soy protein and safflower-seed oil may counteract HUA-related inflammation, alleviate monocyte activation, and enhance Th2 immune response in HUA. A plant-based diet rich in soy protein and safflower-seed oil may help manage HUA and associated inflammation and immune dysfunction. Full article

κ-casein (CSN3) polymorphisms are closely related to productive performance and dairy processing performance. In this study, CSN3 3’UTR polymorphisms in Chinese Holstein cows (n = 50) and the effects of these polymorphisms on the gene expression of four caseins, the protein expression of κ-casein, the binding of microRNAs (miRNAs), and cow production performance were investigated. There were two main haplotypes for the CSN3 3’UTR in Chinese Holstein cows: Haplotype 1 (0 mutations, n = 16) and Haplotype 10 (a combination of 7 mutations, n = 17). The gene and protein expression levels of CSN3 in Haplotype 1 were significantly greater than those in Haplotype 10 (p < 0.05). The ability of bta-miR-708 to bind to the CSN3 3’UTR with Haplotype 10 was significantly greater than that with Haplotype 1 (p < 0.05), potentially explaining why the gene and protein expression of CSN3 with Haplotype 10 were lower than those with Haplotype 1. Dairy herd improvement (DHI) data, including 305-d milk production, fat-corrected milk, fat (%), protein (%), and fat/protein ratio, were not significantly different between the two haplotypes (p > 0.05). Results suggest that the two major CSN3 3’UTR polymorphisms in Chinese Holstein cows cause significant changes in CSN3 gene expression, CSN3 protein expression, and bta-miR-708 binding ability but no significant alterations in macroscopic DHI data. Therefore, CSN3 3’UTR polymorphisms should be investigated further. Full article

Sanxan (SAN) is a novel microbial polysaccharide that is both safe and edible and represents a promising new source of food resources. It exhibits gelling properties and certain emulsifying properties. To date, there have been few studies published on the enhancement of protein emulsification by sanxan. In this study, three widely used proteins were used: casein (CS), pea protein isolate (PPI), and soy protein isolate (SPI). SAN–protein composite particles were prepared by non-covalent interactions to evaluate the availability of SAN in Pickering emulsions. The effect of SAN on the ability of the complexes to stabilize the emulsion was investigated by measuring and characterizing the physicochemical properties of three SAN–protein complexes. Fourier transform infrared (FTIR) and fluorescence spectroscopy analyses showed that SAN was able to bind to three proteins to form complexes. All three complexes formed by SAN with SPI, PPI and CS had good emulsification properties, with PPI-SAN being the best. Storage results showed better stability of the composite particle-stabilized emulsion. These results indicate that the complexation of SAN with proteins improves the emulsification of proteins and increases the stability of Pickering emulsions. The findings of this study provide valuable information for the utilization of SAN in emulsions. Full article

The influence of heating as a pretreatment on the structural and functional attributes of milk protein concentrate (MPC) powders derived from ultrafiltered/diafiltered (UF/DF) skim milk is under-reported. This research delves into the impact of pH and heat treatment on skim milk’s properties before UF/DF and how these changes affect the resulting MPC powders. By adjusting the pH of skim milk to 6.5, 6.8, or 7.1 and applying thermal treatment at 90 °C for 15 min to one of two divided lots (with the other serving as a control), we studied the protein interactions in MPC. Post-heat treatment, the skim milk’s pH was adjusted back to 6.8, followed by ultrafiltration and spray drying to produce MPC powders with protein content of 82.38 ± 2.72% on a dry matter basis. MPC dispersions from these powders at 5% protein (w/w) were also evaluated for particle size, viscosity, and heat coagulation time (HCT) to further understand how the protein interactions in skim milk influence the properties of MPC dispersions. Capillary electrophoresis was used to assess the casein and whey protein distribution in both the soluble and colloidal phases. Findings revealed that preheating skim milk at pH 7.1 increased serum phase interactions, while heating skim milk preadjusted to a pH of 6.5 promoted whey protein–casein interactions at the micellar interface. Notably, the D (4,3) of casein micelles was larger for dispersions from milk with a preheated pH of 6.5 compared to other pH levels, correlating positively with enhanced dispersion viscosity due to increased volume fraction. These results support the potential for tailoring MPC powder functionality in various food applications through the precise control of the milk’s pre-treatment conditions. Full article