Effect of heat treatments on foaming and physico-chemical properties of bovine and camel sodium caseinate.

The objective of this study was to examine the foaming properties of sodium caseinates (Na-cas) extracted from bovine and camel fresh milks after heating at 70, 80, 90 and 100°C for 30 min at laboratory scale. Experimental results indicated that greater foam was obtained with camel Na-cas than with bovine Na-cas at all heating temperatures due to the higher ß-casein content in camel caseins (~53.4% of total proteins, RP-HPLC results). Increasing heat-treatment temperature to 100°C significantly enhanced the foaming properties by raising surface hydrophobicity and decreasing electronegative charge as well as interfacial tension values upon heating. This study concluded that camel Na-cas has important foaming properties in agricultural and food industries.

Recent advances in selective allergies to mammalian milk proteins not associated with Cow's Milk Proteins Allergy.

Cow's milk proteins allergy (CMA) is an atypical immune system response to cow's milk and dairy products. It's one of the most common food allergies in children affecting 8% of the total pediatric population pediatric population. This comprehensive review examines recent studies in CMA, especially regarding mammalian milk allergies such as goat's, sheep's, buffalo's, camel's, mare's and donkey's milk allergies in order to increase awareness of these selective allergies and to reduce allergy risks for those who have them. The consumption of other mammalian milk types is not recommended because of the significant homology between milk proteins from cow, sheep, goat and buffalo resulting in clinical cross-reactivity. However, camel's, mare's or donkey's milk may be tolerated by some allergic patients. Selective mammalian milk allergies are unusual and rare disorders characterized by severe symptoms including angio-oedema, urticaria, respiratory manifestations and anaphylaxis. Based on the reported allergic cases, cheese products including Ricotta, Romano, Pecorino and Mozzarella, are considered as the most common source of allergens especially in goat's, sheep's and buffalo's milk allergies, while the major allergens in donkey's and mare's milk seems to be whey proteins including lysozyme, α-lactalbumin and ß-lactogloblin due to the low casein/whey proteins ratio in equine's milk.

Comparison of Ethanol Stability and Chemical Composition of Camel Milk from Five Samples.

This research was carried out to study the variation in ethanol stability and chemical composition of five camel milk samples, including two pasteurized samples (Alwatania and Darir alabaker) and three raw samples (Majaheim, Wadah, and Hamra). Ethanol stability was analyzed by dispersing camel milk samples with 0 to 100% ethanol (v/v). The findings indicate that camel milk samples precipitated after adding an equal volume of ethanol at concentrations between 50% and 64% ethanol, depending on the milk sample. The addition of sodium chloride at different concentrations (1−10%) to camel milk resulted in a significant increase in ethanol stability, and samples from Majaheim and Alwatania exhibited the highest ethanol stability values (88%). In contrast, the addition of EDTA to camel milk for pH ranging between 5.9 and 7.1 has increased ethanol stability with a sigmoidal shape in camel milk. The largest ethanol stability differences were observed in a camel milk sample from Alwatania. Thus, the level of Ca2+ in camel milk may contribute to ethanol stability by shifting the entire profile to higher ethanol stability values. The chemical composition of different camel samples was also determined. The lactose content of camel milk varied significantly (p < 0.05) across samples, ranging from 4.37% in Majaheim camel milk to 4.87% in Alwatania camel milk. The total solids of camel milk varied significantly between raw and pasteurized samples, ranging between 10.17% and 12.10%. Furthermore, protein concentration in camel milk obtained from different camel samples varied, from 2.43% to 3.23% for Hamra and Alwatania, respectively. In conclusion, ethanol stability in camel milk was dependent on the camel breed, pH level, ionic strength, and EDTA addition.

Physicochemical, techno-functional, and fat melting properties of spray-dried camel and bovine milk powders.

In this study, three skimmed and one whole-fat spray-dried camel milk powders were produced and their characteristics were compared to those of bovine milk powders. The physicochemical analysis of the produced powders indicated that camel milk powders (whether skimmed or not) presented higher ash and whey protein contents as compared to those of bovine milk powders. Our results indicated that the investigated camel and bovine milk powders exhibited a high solubility index (>99%) with poor dispersibility and wettability indexes due to their small particles size (d50 ≤ 12 µm) and their narrow size distribution (span ≤ 2). In addition, although camel and bovine milk powders presented the same total fat content, lower free fat content was measured for camel milk powders. Besides, the whey protein nitrogen index and the SDS-PAGE electrophoresis underlined that camel and bovine milk proteins remained intact after drying with low denaturation extent. It is worth noticed that camel milk proteins were less denaturized due to the absence of the heat-sensitive ß-lactoglobulin in camel milk. Moreover, the low denaturation extent participated in the enhancing of the foaming capacity and stability of camel and bovine milk powders. Finally, the calorimetric analysis showed that higher fat melting temperatures were recorded in whole-fat camel milk powder and in their anhydrous form as compared to those of bovine milk. PRACTICAL APPLICATION: Camel milk powder is an emerging non-bovine dairy product. Understanding its rehydration ability and evaluating the impact of spray drying on its protein quality are promising approaches to obtain high-quality camel milk powder with high reconstitution ability. Findings of this study indicated that spray drying is a suitable technique to produce highly soluble camel milk powders with low denaturation extent. These results will benefit the research and development department of food industry (especially those producing camel milk powder) as well as the direct consumers.

Camel α-lactalbumin at the oil-water interface: Effect of protein concentration and pH change on surface characteristics and emulsifying properties.

Camel α-lactalbumin (Ala-C), the main whey protein of camel milk, was purified by membrane filtration. Surface hydrophobicity as well as interfacial tension were examined at different levels of pH (3.0, 6.0, 9.0) and protein concentration (0.1 %, 0.2 %, 0.4 % w/w), and compared to bovine α-lactalbumin (Ala-B). The emulsifying properties (EAI and ESI) of oil-in-water emulsions (20 %/80 %) were investigated for both proteins. The stability of the processed emulsions was characterised by ζ-potential, particle size and viscosity measurements. The main findings indicate that Ala-C exhibited greater surface hydrophobicity and undergone changes in conformational structure when pH decreased from 9.0-3.0. These changes were enhanced by increasing protein concentration from 0.1 % to 0.4 % (w/w). However, high concentrations showed low emulsifying activity, especially at pH 6.0 where interfacial tension was lower. In comparison with Ala-B, maximum EAI was close, despite the lower surface hydrophobicity of Ala-C under similar conditions. Overall, emulsions were more viscous at pH 3.0 due to the greater surface coverage than at 9.0 and 6.0. Under the conditions of this study, a protein concentration of 0.2 % resulted in the finest oil droplets and highest viscosity for both types of α-lactalbumin, and Ala-C conferred the highest long-term stability to the emulsions.

Antioxidant and antibacterial activities, interfacial and emulsifying properties of the apo and holo forms of purified camel and bovine α-lactalbumin.

The antioxidant and antibacterial activities of camel and bovine α-lactalbumin (α-La) in both calcium-loaded (holo) and calcium-depleted (apo) forms were investigated and compared. Antioxidant assay showed that camel and bovine α-La exhibited significant Ferric-reducing antioxidant power (FRAP), ferrous iron-chelating activity (FCA) and antiradical activities especially in their apo form. Camel apo α-La also exhibited attractive antibacterial activities against Gram-negative bacteria (Pseudomonas aeruginosa) and against fungal pathogens species (Penicillium bilaiae, Aspergillus tamari and Aspergillus sclerotiorum). Likewise, emulsifying properties (emulsification ability (EAI) and stability (ESI) indexes) and the surface characteristics (surface hydrophobicity, ζ-potential and interfacial tension) of the α-La were assessed. Maximum EAI were found at pH 7.0, with higher EAI values for the camel apo α-La (EAI ~19.5 m2/g). This behavior was explained by its relative high surface hydrophobicity and its greater efficiency to reduce the surface tension at the oil-water interface. Furthermore, emulsions were found to be more stable at pH 7.0 compared to pH 5.0 (ESI ~50%) due to the higher electrostatic repulsive forces between oil droplets at pH 7.0 in consistence with the ζ-potential results. This study concluded that the camel apo α-La has antibacterial, antioxidant, and emulsifying properties in agricultural and food industries.

The foaming properties of camel and bovine whey: The impact of pH and heat treatment.

The effect of heat treatment (70°C or 90°C for 30min) on the foaming and interfacial properties of acid and sweet whey obtained from bovine and camel fresh milk was examined. The maximum foamability and foam stability were observed for acid whey when compared to sweet whey for both milks, with higher values for the camel whey. This behavior for acid whey was explained by the proximity of the pI of whey protein (4.9-5.2), where proteins were found to carry the lowest negative charge as confirmed by the zeta potential measurements. Interfacial properties of acid camel whey and acid bovine whey were preserved at air water interface even after a heat treatment at 90°C. These results confirmed the pronounced foaming and interfacial properties of acid camel whey, even if acid and sweet bovine whey exhibited the highest viscoelastic modulus after heating.

The effect of pH and heat treatments on the foaming properties of purified α-lactalbumin from camel milk.

The effect of pH (4.3 or 6.5) and heat treatment (70°C or 90°C for 30min) on the foaming and interfacial properties of α-lactalbumin extracted from camel milk were studied. The increased temperature treatment changed the foaming properties of camel α-lactalbumin solution and its ability to unfold at the air-water interface. At neutral pH, heat treatment was found to improve foamability, whereas at acid pH (4.3) this property decreased. Foams were more stable after a heat treatment at pH 4.3 than at 6.5, due to higher levels of protein aggregation at low pH. Heat treatment at 90°C for 30min affected the physicochemical properties of the camel α-lactalbumin by increasing free thiol group concentration at pH 6.5. Heat treatment also caused changes in α-lactalbumin's surface charge. These results also confirm the pronounced aggregation of heated camel α-lactalbumin solution at acid pH.

Foaming and adsorption behavior of bovine and camel proteins mixed layers at the air/water interface.

The aim of this work was to examine foaming and interfacial behavior of three milk protein mixtures, bovine α-lactalbumin-ß-casein (M1), camel α-lactalbumin-ß-casein (M2) and ß-lactoglobulin-ß-casein (M3), alone and in binary mixtures, at the air/water interface in order to better understand the foaming properties of bovine and camel milks. Different mixture ratios (100:0; 75:25; 50:50; 25:75; 0:100) were used during foaming tests and interfacial protein interactions were studied with a pendant drop tensiometer. Experimental results evidenced that the greatest foam was obtained with a higher ß-casein amount in all camel and bovine mixtures. Good correlation was observed with the adsorption and the interfacial rheological properties of camel and bovine protein mixtures. The proteins adsorbed layers are mainly affected by the presence of ß-casein molecules, which are probably the most abundant protein at interface and the most efficient in reducing the interfacial properties. In contrast of, the globular proteins, α-lactalbumin and ß-lactoglobulin that are involved in the protein layer composition, but could not compact well at the interface to ensure foams creation and stabilization because of their rigid molecular structure.