Effect of starter cultures on properties of soft white cheese made from camel (Camelus dromedarius) milk

This experiment was conducted to investigate the effect of starter cultures on the physicochemical properties, texture, and consumer preferences of soft white cheese (SWC) made from camel (Camelus dromedarius) milk. The experiment was laid out in a completely randomized design with 5 treatments [starter cultures; i.e., 1 thermophilic (STI-12), 2 blended (RST-743 and XPL-2), and 2 mesophilic (R-707 and CHN-22) cultures]. Starter cultures STI-12 and RST-743 were inoculated at 37°C, whereas XPL-2, R-707, and CHN-22 were inoculated at 30°C. Camel milk inoculated using STI-12 and RST-743 cultures resulted in faster acidification than XPL-2, R-707, and CHN-22 cultures. Camel milk SWC made using STI-12 and CHN-22 cultures gave lower pH (4.54) and titratable acidity (0.59), respectively, whereas R-707 culture resulted in high cheese yield (13.44 g/100 g). In addition, high fat (20.91 g/100 g), protein (17.49 g/100 g), total solids (43.44 g/100 g), and ash (2.40 g/100 g) contents were recorded for SWC made from camel milk made using RST-743 culture. Instrumental analysis of cheese texture revealed differences in resistance to deformation in which camel milk SWC made using RST-743 culture gave higher firmness (3.20 N) and brittleness (3.12 N). However, no significant difference was observed among camel milk SWC adhesiveness made using different starter cultures. Consumer preference for appearance, aroma, taste, and overall acceptances of SWC were affected by inoculation of starter cultures. Considering curd firmness, cheese yield, compositional quality, and textures using STI-12, RST-743, and R-707, these cultures were found to be better for the manufacture of camel milk SWC.     

Stereospecific analysis of triacylglycerols in camel (Camelus dromedarius) milk fat

In the lipid fraction of camel (Camelus dromedarius) milk the percentage of saturated fatty acids (SFAs) was 62.8% with a content of palmitic acid of 28.5%. The unsaturated fatty acid (UFA) fraction was dominated by oleic and palmitoleic acids. Enzyme digestion and chemical degradation methods were used to determine the intramolecular fatty acid (FA) composition and then the intermolecular FA distribution in the three sn-positions of the triacylglycerols of the camel milk. FAs showed a specific preference for a particular position: in all samples studied, SFAs were prevalently esterified in the sn-2 position, while UFAs occupied mainly the sn-1 and sn-3 position. As the carbon chain lengthened from 8 to 16 the percentages of SFAs decreased in the sn-2 position and increased in the outer positions. Such data indicated that the length of the carbon chain could be a discriminating factor in the acylation process of SFAs.     

Immunochemical quantification of heat denaturation of camel ( Camelus dromedarius ) whey proteins

The major whey proteins IgG, serum albumin and alpha-lactalbumin were purified from camel milk using gel permeation and ion-exchange chromatography. Specific antisera against each of them were raised and used to quantify their heat denaturation in early or mature milk over a range of 60-90 degrees C for 10-60 min using the single radial immunodiffusion technique. The heat denaturation midpoints for the mature milk heated 30 min were 67.2, 73.0 and 77.5 degrees C for IgG, albumin and alpha-lactalbumin respectively. The early milk was more sensitive to heat treatment with coagulation at low temperature and heat denaturation midpoints of 64.8, 71.6 and 72.6 degrees C respectively. This difference was related to the high IgG content of the early milk (12.6 mg/ml v. 0.5 mg/ml for the mature milk) and stresses the importance of monitoring the IgG level of milk to assess the absence of colostrum.     

Influence of proteolytic Lactococcus lactis subsp. cremoris on ripening of reduced-fat Cheddar cheese made with camel chymosin

This study investigated proteolysis in reduced-fat Cheddar cheese produced with camel chymosin and Lactococcus lactis subsp. cremoris with the ability to cleave the N-terminus of α_S1-casein. The aim was to match the activity of bovine chymosin, which leads to softer cheese structure than camel chymosin. Cheeses were analysed for gross composition, casein and peptide breakdown, release of free amino acids, structure parameters and sensory characteristics. Selected Lc. lactis subsp. cremoris increased the amount of peptides and, to a limited extent, the total amount of free amino acids in the cheeses. One group of experimental cheeses was found to have a significantly firmer structure, higher stress at fracture and modulus of deformability than the reference cheeses. The addition of the selected proteolytic dairy strains of Lc. lactis subsp. cremoris to the cheeses did not result in extended breakdown of α_S1-casein or a softer cheese structure.     

Chemical characterisation of oligosaccharides in commercially pasteurised dromedary camel (Camelus dromedarius) milk

It has been suggested that bactrian camel milk and colostrum may be a good source of biologically significant oligosaccharides but, although the oligosaccharides found in bactrian camel milk and colostrum have been characterised, those in dromedary camel milk have not. In this study, seven oligosaccharides from commercially available pasteurised dromedary camel milk were characterised using ¹H nuclear magnetic resonance spectroscopy. The following oligosaccharides were detected: Gal(β1-3)Gal(β1-4)Glc (3′-galactosyllactose), Gal(β1-4)GlcNAc(β1-3)[Gal(β1-4)GlcNAc(β1-6)]Gal(β1-4)Glc (lacto-N-neohexaose), Neu5Ac(α2-3)Gal(β1-4)Glc (3′-sialyllactose), Neu5Ac(α2-6)Gal(β1-4)Glc (6′-sialyllactose), Neu5Ac(α2-3)Gal(β1-3)Gal(β1-4)Glc (sialyl-3′-galactosyllactose), Neu5Ac(α2-3)Gal(β1-3)[Gal(β1-4)GlcNAc(β1-6)]Gal(β1-4)Glc (sialyllacto-N-novopentaose a) and Neu5Ac(α2-6)Gal(β1-4)GlcNAc(β1-3)[Gal(β1-4)GlcNAc(β1-6)]Gal(β1-4)Glc (monosialyllacto-N-neohexaose).     

Comparison of uteroplacental glycosylation in the camel (Camelus dromedarius) and alpaca (Lama pacos)

The recent birth of a camel-llama hybrid, after numerous failed attempts, has prompted an investigation into the glycosylation of apposing fetal and maternal tissues of pregnant camels and alpacas. This study was undertaken to determine whether interspecies differences in glycans are factors that may account in part for the difficulty in producing a viable hybrid. Specimens of camel placentae from day 60 to day 375 of gestation and alpaca placentae from day 22 to term (approximately 345 days) were fixed and embedded in resin, and sections were stained with a panel of 19 biotinylated lectins and an avidin--peroxidase revealing system. Several qualitative interspecies differences in tissue glycosylation were found, mainly in the trophoblast, and especially with respect to bi/tri-antennary bisected N-glycan, fucosylated structures, beta-galactosyl residues and sialyl termini. In the maternal uterine epithelium, differences were found mainly in bi/tri-antennary bisected complex N-glycan and beta-galactosyl residues, indicating that there is more conservation of glycosylation in maternal tissues compared with trophoblast. There were also many quantitative differences in the distribution of glycans. It is possible that a failure to effect the normal glycan--glycan complementation that occurs at the cell surface between maternal and fetal tissues during the implantation processes of apposition and adhesion may account in part for the difficulty in establishing a viable pregnancy between these two species.     

Studies on the supply of immunoglobulin G to newborn camel calves (Camelus dromedarius)

A major problem in camel productivity is the high mortality rate of camel calves in the first 3 months. The causes for mortality are mainly poor management practice and infectious diseases. The purpose of this research, carried out on a ranch in Kenya, was to determine the immunoglobulin G (IgG) concentration in camel colostrum as well as the extent of the calves' passive immunization by maternal antibodies. IgG concentration in colostrum and in the serum of the calf were measured during the first 3 d of life. Evaluation was carried out by comparing the respective values with those for horses and cattle. The average IgG concentration in the camel colostrum was higher than that found in literature for horses and cattle. IgG concentration in the serum of the camel calves reached its maximum 24 h after birth. In 39% of the examined calves, this maximum concentration was below 4 g/l, which is considered to be the critical value in horses and cattle. 61% of the calves achieved an IgG concentration of over 4 g/l. Since there is no correlation between IgG level in colostrum and early mortality, the results indicate that low colostrum intake during the first 24 h of life and not low IgG concentration in colostrum is presumably one of the main causes of early calf mortality. Therefore, it was recommended that the care of the newborn calves by herdsmen should be improved.     

Effect of season on contractile and metabolic properties of desert camel muscle (Camelus dromedarius)

Thirty fattened one humped desert camels were used to examine the effect of season on contractile and metabolic properties of Longissimus thoracis (LT) muscle. Ten camels were slaughtered according to seasons of the year (winter, summer and autumn). Season significantly influenced muscle chemical composition, ultimate pH (pHu) and color. Activities of metabolic enzymes were higher during autumn season compared to summer and winter for phosphofructokinase (+ 64% compared to both seasons) and for isocitrate dehydrogenase (+ 35% and + 145% in autumn vs. summer and winter, respectively). Quantification of muscle myosin heavy chain isoforms by SDS-PAGE electrophoresis showed only presence of type I and type IIa MyHC in camel muscle and indicated high proportion in winter for type I and in autumn for type IIa with respect to other seasons. Several correlations between different MyHC proportions and enzyme activities were reported. These findings indicated that muscle characteristics in camels are influenced by season.     

Milk production and feeding behavior in the camel (Camelus dromedarius) during 4 watering regimens

Camels survive and produce milk during recurrent prolonged hot and dry periods. The objective was to evaluate how different watering intervals affected milk production and feeding. Eight lactating camels (Camelus dromedarius) were recruited and subjected to 4 watering regimens in a Latin square design experiment performed at Haramaya University in Ethiopia. Each regimen lasted 16 d with 5 d of daily watering between periods: water was offered at 1315 h once daily (W1); on d 4, 8, 12, and 16 (W4); on d 8 and 16 (W8); and on d 16 (W16). One camel became sick in the second period and its results were excluded. Camels were kept in a pen with minimal shade and a noon temperature of 30.9 ± 0.1°C. They had free access to hay and were offered 2 kg of concentrates 3 times daily. At noon on d 1, 4, 8, 12, and 16, a blood sample was taken from the jugular vein before watering. All calves were kept together in a separate pen. Morning and afternoon calves stimulated milk let-down before the camels were hand-milked, after which the calves suckled, emptying the udder. Camels maintained the milk volume during water deprivation for about 1 wk, but they produced less milk during the second week during W16. Morning milk osmolality increased from 315 ± 3 on d 1 to 333 ± 3 mosm/kg on d 4 during W4 and from 321 ± 3 on d 1 to 342 ± 3 mosm/kg on d 8 during W8. After watering at 1315 h, milk osmolality decreased to 316 ± 3 and 323 ± 3 mosm/kg, respectively, the same afternoon and then increased during recurrent water deprivation to 338 ± 3 (W4) and 347 ± 3 mosm/kg (W8) on d 16, respectively. During W16, osmolality increased from 318 ± 3 to 336 ± 3 mosm/kg during the first 4 d of water deprivation, but during the remaining 12 d the further rise in osmolality was not higher compared with that on d 4. The change in milk osmolality was linearly correlated to plasma osmolality (r = 0.8), but milk lactose content did not increase. Contrary to widespread belief, camels did not dilute their milk when dehydrated. Instead milk osmolality increased in parallel to blood osmolality. This study provides further support to earlier observations on camels’ adaptation to their environment.     

Angiotensin converting enzyme‐inhibitory activity and antimicrobial effect of fermented camel milk (Camelus dromedarius)

This study aimed to determine the angiotensin converting enzyme‐inhibitory activity and antimicrobial effect of fermented camel milk. Samples were prepared either using Lactobacillus acidophilus and Streptococcus thermophilus or Lactobacillus helveticus and Str. thermophilus and labelled as S1 and S2, respectively. The IC₅₀ values of S1 and S2 samples ranged between 113–200 and 70–133 μg/mL, respectively. The antimicrobial effects of S1 and S2 samples against Bacillus cereus, Salmonella Typhimurium and Staphylococcus aureus were apparent after 12 h of incubation and continued until 15 days of storage, whereas unfermented camel milk exhibited no antimicrobial effects against any of the tested pathogens.     

Alternative splicing of lactophorin mRNA from lactating mammary gland of the camel (Camelus dromedarius).

The objective of this study was to determine the corrected structure of lactophorin, a major whey protein in camel milk. The protein had 60.4% amino acid sequence identity to a proteose peptone component 3 protein from bovine whey and 30.3% identity to the glycosylation-dependent cell adhesion molecule 1 in mice. The N-terminal heterogeneity of the protein was a result of alternative mRNA splicing. About 75% of the protein was expressed as a long variant A with 137 amino acid residues and a molecular mass of 15.7 kDa; about 25% was as a short variant B with 122 amino acid residues and a molecular mass of 13.8 kDa. Both proteins are probably threefold phosphorylated. In contrast to the related proteins, no glycosylation was found in camel lactophorin. Because of this difference, specific interaction with carbohydrate binding proteins, as reported for the murine protein, can be excluded, and a function of the protein other than cell recognition or rotaviral inhibition is proposed. The concentration of lactophorin in camel milk was found to be about three times higher than the concentration of the bovine homologue in bovine milk. Pronounced similarities existed between the primary and secondary structures of bovine and camel proteins. We speculated that camel lactophorin has a similar function to that of bovine protein in milk, which is supposed to be the prevention of fat globule aggregation and the inhibition of spontaneous lipolysis by lipoprotein lipase.     

Biochemical and molecular characterization of polymorphisms of αs1-casein in Sudanese camel (Camelus dromedarius) milk

This work was designed to detect occurrence of biochemical polymorphism of α_s1-casein in two ecotypes of Sudanese camel (Camelus dromedarius) and to characterize these variants on molecular level. Milk samples were screened for α_s1-casein variability by isoelectric focusing, using skimmed milk, as well as isolated α_s1-casein. Two protein patterns, named α_s1-casein A and C, were identified, whereas the major allele A revealed frequencies of 0.8214 and 0.8615 in the two ecotypes. CSN1S1*A and CSN1S1*C are both characterized by missing of exon 16 on mRNA-level compared with the previously described CSN1S1*B. However, the sequence of exon 16 occurs on DNA-level in both. Therefore, this exon seems to be skipped out during mRNA-processing. Furthermore, CSN1S1*C shows a single G > T nucleotide substitution in exon 5, leading to a non-synonymous amino acid exchange (p.Glu30 > Asp30; GenBank ID: JF429138). A polymerase chain reaction-restriction fragment length polymorphism-method was established as a DNA-based test for this nucleotide substitution.     

Effects of age on fatty acid composition of the hump and abdomen depot fats of the Arabian camel (Camelus dromedarius)

This study aimed to quantify concentrations of fatty acids in the hump and abdomen fats of three different age groups of camel. Hump and abdomen fats were extracted from eight each of one-humped camels (Camelus dromedarius) of three age groups: group 1 (<1 year old), group 2 (1-3 years old) and group 3 (>3 years old). The fatty acid methyl ester concentrations of these fats were determined by gas-liquid chromatography (GLC). The percentage of fat in the hump (H) and abdomen (A) fats was significantly (P<0.05) lower for group 1 (H 92.0% and A 94.3%) than for group 2 (H 97.4% and A 97.2%) and group 3 (H 97.6% and A 97.5%), on a dry matter basis. Hump and abdomen fats from the three different groups had similar fatty acid patterns with more saturated than unsaturated fatty acids. The saturated fatty acids in the hump fats accounted for 58.3, 67.6, and 63.0% of the total fatty acids for groups 1, 2 and 3, respectively; group 1 had significantly (P<0.05) lower saturated and higher unsaturated fatty acid concentrations than group 2. The iodine numbers were significantly (P<0.05) higher in group 1 than either group 2 or 3. Palmitic acid (C16:0) was the major fatty acid in hump fat with 32.06, 32.90 and 34.37%, followed by oleic acid (C18:1) 33.65, 21.66 and 28.91.0% and stearic acid (C18:0) 18.85, 24.13 and 20.74% for groups 1, 2 and 3, respectively. Group 1 had significantly higher (P<0.05) oleic acid and lower stearic acid concentrations than group 2. The melting point of both hump and abdomen fats varied between the age groups. This study indicated that age has an effect on the fatty acid composition and the melting point of hump and abdomen fats in one-humped Arabian camels.     

Applicability of a bacteriocin-producing Enterococcus faecium as a co-culture in Cheddar cheese manufacture

Two strains, Enterococcus faecium RZS C5 and E. faecium DPC 1146, produce listericidal bacteriocins, so-called enterocins. E. faecium RZS C5 was studied during batch fermentation in both a complex medium (MRS) and in milk to understand the influence of environmental factors, characteristic for milk and cheese, on both growth and bacteriocin production. Fermentation conditions were chosen in view of the applicability of in situ enterocin production during Cheddar cheese production. Enterocin production by E. faecium RZS C5 in MRS started in the early logarithmic growth phase, and enterocin activity decreased during the stationary phase. The effect of pH on enterocin production and decrease of activity was as intense as the effect on bacterial growth. Higher enterocin production took place at pH 5.5 compared with pH 6.5. The use of lactose instead of glucose increased the production of enterocin, and at higher lactose concentration, production increased more and loss of activity decreased. The production in skimmed milk compared to MRS was lower and was detected mainly in the stationary phase. When casein hydrolysate was added to the milk, enterocin production was higher and started earlier, indicating the importance of an additional nitrogen source for growth of E. faecium in milk. For co-cultures of E. faecium RZS C5 with the starters used during Cheddar cheese manufacture, no enterocin activity was detected during the milk fermentation. Furthermore, the applicability of E. faecium RZS C5 and E. faecium DPC 1146 strains was tested in Cheddar cheese manufacture on pilot scale. Enterocin production took place from the beginning of the cheese manufacturing and was stable during the whole ripening phase of the cheese. This indicates that both an early and late contamination of the milk or cheese can be combated with a stable, in situ enterocin production. The use of such a co-culture is an additional safety provision beyond good manufacturing practices.     

Lactoferrin and immunoglobulin contents in camel's milk (Camelus bactrianus, Camelus dromedarius, and Hybrids) from Kazakhstan

Lactoferrin (Lf) and IgG were estimated in camel's milk from Kazakhstan, where 2 species of camels (Camelus bactrianus, Camelus dromedarius) and their hybrids cohabit. The concentrations of Lf and IgG were determined according to 3 variation factors: region (n = 4), season (n = 4), and species (n = 5; sample 4 was mixed milk and sample 5 was of unknown origin). The mean values in raw camel's milk were 0.229 ± 0.135 mg/mL for Lf concentration and 0.718 ± 0.330 mg/mL for IgG concentration. The seasonal effect was the only significant variation factor observed, with the highest values in the spring for Lf and in the winter for IgG. The Lf concentration varied in 1-wk postpartum milk from 1.422 to 0.586 mg/mL. The range in IgG concentration was wide and decreased from 132 to 4.75 mg/mL throughout the 7 d postpartum, with an important drop after parturition. In fermented milk, the lactoproteins are generally hydrolyzed. For milk samples from undefined species, discriminant analyses did not allow the origin of the species to be determined. A slight correlation between Lf and IgG concentrations was observed in raw milk. The values were slightly higher than those reported in cow's milk, but this difference was insufficient to attribute medicinal virtues to camel's milk.     

Effect of camel chymosin on the texture,functionality, and sensory properties of low-moisture,part-skim Mozzarella cheese

The objective of this study was to compare the effect of coagulant (bovine calf chymosin, BCC, or camel chymosin, CC), on the functional and sensory properties and performance shelf-life of low-moisture, part-skim (LMPS) Mozzarella. Both chymosins were used at 2 levels [0.05 and 0.037 international milk clotting units (IMCU)/mL], and clotting temperature was varied to achieve similar gelation times for each treatment (as this also affects cheese properties). Functionality was assessed at various cheese ages using dynamic low-amplitude oscillatory rheology and performance of baked cheese on pizza. Cheese composition was not significantly different between treatments. The level of total calcium or insoluble (INSOL) calcium did not differ significantly among the cheeses initially or during ripening. Proteolysis in cheese made with BCC was higher than in cheeses made with CC. At 84 d of ripening, maximum loss tangent values were not significantly different in the cheeses, suggesting that these cheeses had similar melt characteristics. After 14 d of cheese ripening, the crossover temperature (loss tangent = 1 or melting temperature) was higher when CC was used as coagulant. This was due to lower proteolysis in the CC cheeses compared with those made with BCC because the pH and INSOL calcium levels were similar in all cheeses. Cheeses made with CC maintained higher hardness values over 84 d of ripening compared with BCC and maintained higher sensory firmness values and adhesiveness of mass scores during ripening. When melted on pizzas, cheese made with CC had lower blister quantity and the cheeses were firmer and chewier. Because the 2 types of cheeses had similar moisture contents, pH values, and INSOL Ca levels, differences in proteolysis were responsible for the firmer and chewier texture of CC cheeses. When cheese performance on baked pizza was analyzed, properties such as blister quantity, strand thickness, hardness, and chewiness were maintained for a longer ripening time than cheeses made with BCC, indicating that use of CC could help to extend the performance shelf-life of LMPS Mozzarella.     

固定化凝乳蛋白酶生产干酪的应用研究

<正> 在干酪的生产中,乳的凝固是通过犊牛第四胃制取的皱胃酶专一地分解K-酪蛋白,即在K-酪蛋白敏感的苯丙氨酸(105)-蛋氨酸(106)肽键处断裂。乳的凝固分两个步骤进行:第一、是从K-酪蛋白分除亲水性的巨肽(106-109位残基部分);第二、是在Ca++影响下将疏水性的1-105位残基组成部分,与其它不稳定的酪蛋白组分相聚而形成凝固的酪蛋白。