Search Results (10)

Consumer demand for dairy products like cheese and curds has resulted in a rise in whey production, which has caused significant waste and environmental issues. For this reason, improving the functional characteristics of whey proteins and their usage value are essential. In this study, camel whey protein–galactose conjugates (CWP-Gal) and camel whey protein–glucose conjugates (CWP-Glu) were prepared through the Maillard reaction, and their structural and functional properties were characterized. Improvements in solubility of 14.90% and 8.17%, emulsification activity of 15.53% and 13.64%, and foaming capacity of 113.95% and 106.03% were demonstrated by CWP-Gal and CWP-Glu in comparison to camel whey protein (CWP). Circular dichroism analysis revealed secondary structure alterations in CWP-Gal and CWP-Glu compared to CWP. SDS-PAGE, FT-IR, and intrinsic fluorescence spectroscopy all verified that sugar molecules and proteins were covalently conjugated. SEM analysis revealed that the conjugates had a more sparsely packed microstructure. The results demonstrate that CWP-Gal exhibits enhanced structural stability and superior functional properties, providing a scientific basis for its potential utilization in the food industry. Full article

Background: Equine milk, including its whey proteins, is a source of nutrients and functional components in the human diet, and is especially beneficial for people with weakened immune systems, newborns, and athletes. Objectives Whey proteins in equine milk constitute approximately 20% of the total protein content and include various fractions such as albumin, globulin, and lactoferrin. Lactoferrin is one of the most extensively studied whey proteins in equine milk. Methods: HPLC-Mass analysis, enzymatic hydrolysis, modeling of 3D structure and biological activity in silico. Results: It has antioxidant, anti-inflammatory, and immunomodulatory properties, making it a promising candidate for influencing the various aspects of cardiovascular disease pathogenesis. The products of Lactoferrin hydrolysis by trypsin were confirmed using HPLC. The half-lives of the hydrolysate in the bloodstream and in an intestine-like environment were predicted in silico. Various biological activities (antihypertensive, anti-inflammatory, and antiangiogenic) were also estimated in silico and compared with the corresponding activities of lactoferrin hydrolysate amino acid sequences from camel and dromedary milk. Conclusions: The three-dimensional modeling of lactoferrin hydrolysate peptides was performed to support the development of computational models or simulations, as well as to investigate their potential antimicrobial, anti-inflammatory, or immune-modulating functions in clinical or nutritional applications. Full article

Camel whey protein (CWP) is a potent natural antioxidant, noted for its abundance of antioxidant amino acids. Despite its promising properties, the precise mechanisms underlying its effects remain inadequately explored. This study aims to investigate the impact of CWP on kidney damage induced by acute heat stress in rats, as well as to elucidate its mechanism of action. We assessed CWP’s influence on cytochrome P450 2J (CYP2J) activity during heat stress, measured oxidative stress levels, and evaluated renal injury using CYP2J knockout rats. Our findings indicate that acute heat stress reduces CYP2J expression, while CWP administration restores CYP2J activity and enhances PI3K/Akt signaling. However, CWP did not mitigate oxidative stress-induced kidney damage in CYP2J^−/− rats, suggesting the necessity of CYP2J for its protective effects. Full article

Follow-on formulas are necessary for newborns that are unable to breastfeed. Thus, the development of formulas more tailored to infants’ needs is highly important. Recently, using camel milk, goat milk, and sweet milk whey in the formulation of follow-on formulas has gained researchers’ attention. Moreover, developing postbiotic systems to create formulas that mimic human milk, are easy to digest, improve compatibility with an infant’s gut, and boost immunity is crucial. Thus, this study aimed to create and assess different formulations using fermented whey from camel and goat milks. The fermentation process involved the use of Lactobacillus helveticus as a probiotic and proteolytic lactic acid bacterium strain. The study monitored the proteolytic activity and antioxidant properties of sweet whey produced from cow, camel, and goat milks during the fermentation process with L. helveticus. Also, three different milk fat blends were recombined using edible vegetable oils (coconut oil, rice bran oil, and canola oil) and then they were used to formulate follow-on formulas with a similar fat composition to human milk. Finally, the prepared formulas were tested for their in vitro digestibility and antioxidant activity before and after digestion. The L. helveticus strain had high proteolytic activity towards whey proteins from all the types of milk used in the study. A fermentation time of 6 h produced a higher proteolytic degree and antioxidant activity than 2 and 4 h of fermentation. No significant differences were observed for proteolytic degree and antioxidant activity between 6 and 12 h of fermentation for the cow, camel, and goat whey samples. Regarding the fat blends, animal milk fat, rice bran oil, and canola oil in a fat combination were essential to provide the required amount of unsaturated fatty acids in the follow-on formulas, especially the linoleic acid–α-linolenic acid (LA:ALA) ratio. Adding coconut oil in small amounts to the follow-on formulas provided the required amounts of saturated fatty acids, especially lauric and meristic acids. The follow-on formula based on cow or goat milk whey fermented with L. helveticus released more free amino acids (mmol tyrosine equivalent mL⁻¹) with high levels of antioxidants compared to unfermented ones. The release of free amino acids in the follow-on formula based on camel milk whey was not affected by fermentation. Our results recommend using L. helveticus in the fermentation of follow-on formulas based on camel and goat whey instead of formulas based on cow milk proteins. Full article

Camel milk powder production is an alternative to preserve the perishable milk for later-date consumption. However, the impacts of dehydration processes on bioactive compounds in camel milk are largely unknown. Hence, the present study attempted to compare the physicochemical properties and protein profiles of camel milk powders produced by different concentration and dehydration processes. Six camel milk powders were produced by freeze- and spray-drying methods in conjunction with two liquid concentration techniques, namely spray dewatering and reverse osmosis. The results of proteomic analysis showed that direct freeze-dried camel milk powder had the least changes in protein profile, followed by direct spray-dried powder. The camel milk powders that underwent concentration processes had more profound changes in their protein profiles. Among the bioactive proteins identified, lactotransferrin and oxidase/peroxidase had the most significant decreases in concentration following processing. On the contrary, glycosylation-dependent cell adhesion molecule 1, peptidoglycan recognition protein 1, and osteopontin increased in concentration. The results revealed that direct freeze drying was the most ideal method for preserving the bioactive proteins during camel milk powder production. However, the freeze-drying technique has cost and scalability constraints, and the current spray-drying technique needs improvement to better retain the bioactivity of camel milk during powder processing. Full article

Camel milk is a rich source of vitamin C, lactic acid bacteria (LAB), beta-caseins and milk whey proteins, including lactoferrin, lysozyme, lactoperoxidase, alpha-lactalbumin and immunoglobulin. The lactoferrin plays a key role in several physiological functions, such as conferring antioxidant, anti-microbial and anti-inflammatory functions in cells. Similarly, the camel milk alpha-lactalbumin has shown greater antioxidative activity because of its higher antioxidant amino acid residues. The antioxidant properties of camel milk have also been ascribed to the structural conformation of its beta-caseins. Upon hydrolysis, the beta-caseins lead to some bioactive peptides having antioxidant activities. Consequently, the vitamin C in camel milk has a significant antioxidant effect and can be used as a source of vitamin C when the climate is harsh. Furthermore, the lysozyme and immunoglobulins in camel milk have anti-microbial and immune regulatory properties. The LAB isolated from camel milk have a protective role against both Gram-positive and -negative bacteria. Moreover, the LAB can be used as a probiotic and may restore the oxidative status caused by various pathogenic bacterial infections. Various diseases such as cancer and hepatitis have been associated with oxidative stress. Camel milk could increase antiproliferative effects and regulate antioxidant genes during cancer and hepatitis, hence ameliorating oxidative stress. In the current review, we have illustrated the anti-microbial and antioxidant properties of camel milk in detail. In addition, the anti-cancer and anti-hepatitis properties of camel milk have also been discussed. Full article

Papain hydrolysis of camel whey protein (CWP) produced CWP hydrolysate (CWPH). Fractionation of CWPH by the size exclusion chromatography (SEC) generated fractions (i.e., SEC-F1 and SEC-F2). The angiotensin converting enzyme inhibitory activity (ACE-IA) and free radical scavenging actions were assessed for CWP, CWPH, SEC-F1, and SEC-F2. The SEC-F2 exerted the highest ACE-IA and scavenging activities, followed by CWPH. The protective effects of CWPH on thioacetamide (TAA)-induced toxicity were investigated in rats. The liver enzymes, protein profile, lipid profile, antioxidant enzyme activities, renal functions, and liver histopathological changes were assessed. Animals with TAA toxicity showed impaired hepatorenal functions, hyperlipidemia, and decreased antioxidant capacity. Treatment by CWPH counteracted the TAA-induced oxidative tissue damage as well as preserved the renal and liver functions, the antioxidative enzyme activities, and the lipid profile, compared to the untreated animals. The current findings demonstrate that the ACE-IA and antioxidative effects of CWPH and its SEC-F2 fraction are worth noting. In addition, the CWPH antioxidative properties counteracted the toxic hepatorenal dysfunctions. It is concluded that the hydrolysis of CWP generates a wide range of bioactive peptides with potent antihypertensive, antioxidant, and hepatorenal protective properties. This opens up new prospects for the therapeutic utilization of CWPH and its fractions in the treatment of oxidative stress-associated health problems, e.g., hypertension and hepatorenal failure. Full article

Antibacterial peptides were isolated and purified from whey proteins of camel milk (CaW) and cow milk (CoW) and their antimicrobial activities were studied. The whey proteins were hydrolyzed using trypsin, and the degree of hydrolysis was identified by gel electrophoresis. The whey hydrolysate (WH) was purified using ultrafiltration and Dextran gel chromatography to obtain small peptides with antibacterial activity. The effect of the antimicrobial peptides on the morphology of bacterial strains was investigated using transmission electron microscopy. Their amino acid composition and antimicrobial activities were then determined. Polypeptides CaWH-III (<3 kDa) and CoWH-III (<3 kDa) had the strongest antibacterial activity. Both Fr.A2 (CaWH-Ⅲ’s fraction 2) and Fr.B1 (CoWH-Ⅲ’s fraction 1) had antibacterial effects toward Escherichia coli and Staphylococcus aureus, with minimum antimicrobial mass concentrations of 65 mg/mL and 130 mg/mL for Fr.A2, and 130 mg/mL and 130 mg/mL for Fr.B1, respectively. The highly active antimicrobial peptides had high amounts of alkaline amino acids (28.13% in camel milk Fr.A2 and 25.07% in the cow milk Fr.B1) and hydrophobic amino acids. (51.29% in camel milk Fr.A2 and 57.69% in the cow milk Fr.B1). This results showed that hydrolysis of CaW and CoW using trypsin produced a variety of effective antimicrobial peptides against selected pathogens, and the antibacterial activity of camel milk whey was slightly higher than that of cow milk whey. Full article

Background: When breastfeeding is impossible or insufficient, the use of cow’s milk-based hypoallergenic infant formulas is an option for infants suffering from or at risk of developing cow’s milk allergy. As the Camelidae family has a large evolutionary distance to the Bovidae family and as camel milk differs from cow’s milk protein composition, there is a growing interest in investigating the suitability of camel milk as an alternative to cow’s milk-based hypoallergenic infant formulas. Methods: The aim of the study was to compare the allergenicity and immunogenicity of camel and cow’s milk as well as investigating their cross-reactivity using a Brown Norway rat model. Rats were immunised intraperitoneally with one of four products: camel milk, cow’s milk, cow’s milk casein or cow’s milk whey fraction. Immunogenicity, sensitising capacity, antibody avidity and cross-reactivity were evaluated by means of different ELISAs. The eliciting capacity was evaluated by an ear swelling test. Results: Camel and cow’s milk showed similarity in their inherent immunogenicity, sensitising and eliciting capacity. Results show that there was a lower cross-reactivity between caseins than between whey proteins from camel and cow’s milk. Conclusions: The study showed that camel and cow’s milk have a low cross-reactivity, indicating a low protein similarity. Results demonstrate that camel milk could be a promising alternative to cow’s milk-based hypoallergenic infant formulas. Full article

Camel milk is consumed in the Middle East because of its high nutritional value. Traditional heating methods and the duration of heating affect the protein content and nutritional quality of the milk. We examined the denaturation of whey proteins in camel milk by assessing the effects of temperature on the whey protein profile at room temperature (RT), moderate heating at 63 °C, and at 98 °C, for 1 h. The qualitative and quantitative variations in the whey proteins before and after heat treatments were determined using quantitative 2D-difference in gel electrophoresis (DIGE)-mass spectrometry. Qualitative gel image analysis revealed a similar spot distribution between samples at RT and those heated at 63 °C, while the spot distribution between RT and samples heated at 98 °C differed. One hundred sixteen protein spots were determined to be significantly different (p < 0.05 and a fold change of ≥1.2) between the non-heated and heated milk samples. Eighty protein spots were decreased in common in both the heat-treated samples and an additional 25 spots were further decreased in the 98 °C sample. The proteins with decreased abundance included serum albumin, lactadherin, fibrinogen β and γ chain, lactotransferrin, active receptor type-2A, arginase-1, glutathione peroxidase-1 and, thiopurine S, etc. Eight protein spots were increased in common to both the samples when compared to RT and included α-lactalbumin, a glycosylation-dependent cell adhesion molecule. Whey proteins present in camel milk were less affected by heating at 63 °C than at 98 °C. This experimental study showed that denaturation increased significantly as the temperature increased from 63 to 98 °C. Full article