Printer Friendly

Chemical composition, nitrogen fractions and amino acids profile of milk from different animal species.

INTRODUCTION

Globally, consumers pay great attention to food and its composition due to a pivotal relationship between diet and human health. Milk is a complex mixture of fat, proteins, carbohydrates, minerals, vitamins and other miscellaneous constituents dispersed in water (Ahmad et al., 2008; Ozrenk and Inci, 2008). The quality of milk products is reliant on milk composition that varies with stage of lactation, milking methods, environment, season, diet, feeding system, breed and species (Kittivachra et al., 2007). However, the composition of milk fluctuates markedly among different species (Pavic et al., 2002; Ahmad et al., 2008). Caseins and whey proteins are the main group of milk proteins found in different ratios in various milk species. Human milk has casein to whey protein ratio of 40:60, quine milk has ratio of 50:50, while cow, sheep, goat and buffalo milk has casein to whey protein of 80:20 (Fox et al., 2000).

Among milk components, proteins are most important constituents of human diet contributing significant nutritional, biological and functional properties. The amino acids profile of caseins and whey proteins occupy a unique position in human nutrition. These proteins are ranked as quality proteins with highest biological value, good digestibility (97% to 98%), rapid absorption and utilization in the body. Specifically, casein is an incredibly efficient nutrient supply owing to its providing a sustained and slow release of amino acids into blood stream (Schaafsma, 2000). The highest concentration of branched chain amino acids (BCAAs) present in milk proteins are important for maintenance of tissue growth, repair and prevention of catabolic actions during exercise. Likewise, the amino acid cysteine enhances glutathione levels, exhibits strong antioxidant properties and assists the body in combating various diseases (Ha and Zemel, 2003). In addition, milk proteins are recognized for their applicability in sports nutrition, baked goods, salad dressings, emulsifiers, infant formulas, and medical nutritional formulas.

Buffalo milk contributes 62.04% of total milk produced in Pakistan while the share of cow, goat, sheep, and camel milk is 34.56%, 1.65%, 0.08%, and 1.81%, respectively (GOP, 2014-15). Milk plays a vital role in building a healthy society and can be used as vehicle for rural development. The importance of milk from non-bovine animals is increasing globally, due to quantity (15% of global milk production) and economical, cultural, and ecological factors. Special nutritional characteristics have been claimed for various types of non-bovine milk and milk products (Al Haj and Al Kanhal, 2010). These underutilized resources are of great significance to milk producers, processors, and consumers for designing the innovative products with versatility, taste and functionality. Hence, valorization of non-bovine milk and milk products requires intensive research, particularly in the area of proteins, peptides and amino acids. Therefore, present research work was carried out on milk composition, protein characterization and amino acid profile of casein and whey proteins with special reference to local milk species found in Pakistan. Purposely, the buffalo (Nili-Ravi), cow (Sahiwal), sheep (Kajli), goat (Beetal), and camel (dromedary) lactating breeds were selected for the study.

MATERIALS AND METHODS

Collection of milk samples

Thirty fresh samples of buffalo, cow, sheep, goat, and camel milk (six samples of each species) were collected in sterile glass bottles from the Dairy Farm, Department of Livestock Management, University of Agriculture, Faisalabad, Pakistan. These samples were labeled, ice packed and transported to laboratory. All milk samples were then placed in the refrigerator at 4[degrees]C for further analysis. Physicochemical analyses were performed (in triplicate) within 24 hours in the Dairy Technology Laboratory, National Institute of Food Science and Technology, University of Agriculture Faisalabad. Freeze-dried samples of caseins and whey proteins were also subjected to estimate their amino acid profile.

Physicochemical analysis

The pH of milk samples was measured using portable pH meter (Hanna, HI-99161). The acidity (%) in sample was estimated by titration method (947.05) given in AOAC (2005). Fat of milk was determined by following Gerber method as described by Marshall (1993). Solid-not-fat (SNF) contents were calculated according to David (1977) using Lactometer. Total solids (TS) were determined according to the method described in AOAC- 925.23 (2005). The ash content was estimated by incineration of samples in muffle furnace at 550[degrees]C for 6 hours, as given in AOAC, No. 945.46 (2005).

Nitrogenous fractions

The crude protein (CP), true protein (TP), casein, non-casein-nitrogen (NCN), whey proteins and non-protein-nitrogen (NPN) contents were determined by using Kjeldahl method according to standard protocol of IDF (1993). After calculating the total amount of nitrogen (%), it was multiplied with a factor 6.38 to get CP. The TP in the milk sample were determined by treating with 12% trichloroacetic acid. The nitrogen (%) was converted to NPN and NCN contents by using the conversion factor 3.60 and 6.25 respectively. Protein (nitrogen) fractions were calculated as:

TP = CP-NPN, Casein (N %) = Total protein (N%)-NCN (N %) Whey protein = NCN-NPN.

Amino acid profiling

Separation of casein and whey proteins: For the separation of caseins and whey proteins, milk samples were defatted by centrifugation at 5,000 g for 15 min at 4[degrees]C. The skim milk, heated to 37[degrees]C, was separated into whole casein and whey proteins by isoelectric precipitation at pH 4.6 with 1 N HCl. After centrifugation at 5,000 g for 15 min at 30[degrees]C, the supernatant (whey proteins), was collected and dialyzed at 4[degrees]C against several changes of distilled water while the precipitated caseins were washed with acidified distilled water (pH 4.6). Both fractions were then freeze-dried for further analysis.

Amino acids analysis: The freeze dried samples of casein and whey protein were then subjected to determination of amino acids composition using an amino acid analyzer according to the method described by Schuster (1988). The freeze-dried samples of casein and whey proteins were hydrolyzed with 6 N HCl under vacuum at 110[degrees]C for 24 hours. The hydrolysates were dried in a rotary evaporator at 40[degrees]C under vacuum to remove the excess acid (6 N HCl). The dry residues were then dissolved in a known quantity of citrate buffer (pH 2.2) and filtered (0.2 pm) to obtain a clean solution of the hydrolysate. An aliquot of hydrolysate was injected into the column (Shim-pack ISC-07/S1504 Na) of the higher performance liquid chromatography based amino acid analyzer (RF-10AXL, Shimadzu Corporation, Tokyo, Japan) equipped with fluorescence detector (FLD-6A). Sodium hypochlorite and o-phthalaldehyde solutions were used as reaction solutions.

Statistical analysis

Statistical analysis of experimental data was performed by applying completely randomized design at 5% level of significance while significant differences between means were compared using Duncan's multiple range test (Steel et al., 1997). The relationship between nitrogen fractions was calculated by simple linear correlations.

RESULTS AND DISCUSSION

Physicochemical analysis of milk samples

The chemical composition of milk samples indicated that fat was the most inconsistent component whereas the ash contents showed minimum variations among different milk species (Table 1). It was observed that sheep milk has maximum fat (6.82% [+ or -] 0.04%), SNF (11.24% [+ or -] 0.02%), TS (18.05% [+ or -] 0.05%) and ash (0.85% [+ or -] 0.01%) contents followed by buffalo milk (6.58% [+ or -] 0.02%), (10.09% [+ or -] 0.03%), (16.67 [+ or -] 0.03%) and (0.82% [+ or -] 0.02%) respectively. Previous studies depicted that Murrah and Nili-Ravi breeds of buffalo milk had 6.57% and 6.53% fat contents respectively (Han et al., 2007). The results regarding TS contents of buffalo, cow, goat and camel milk are also comparable to previously reported results of Han et al. (2007) and Mal et al. (2007). Several factors such as breed and health of animal, stage of lactation, feeding systems, seasonal changes, milking frequency and milking systems, nutrition and genetics can cause variation in relative proportion of milk constituents. Non-significant differences were observed for acidity of milk samples from all species, however, there was some variation in pH values. Milk pH is the most critical factor for manufacturing of various dairy products. It determines the conformation of proteins, the activity of enzymes and dissociation of acids present in milk. The lower pH of fresh milk may be due to bacterial action and higher one indicates the udder infection or mastitis (Uallah et al., 2005). Many previous findings regarding pH and acidity of buffalo milk (Han et al., 2007; Ahmad et al., 2008; Imran et al., 2008), cow milk (Ozrenk and Inci, 2008) and camel milk (Khaskheli et al., 2005; Mal et al., 2007) are in agreement with the findings of current investigation.

Nitrogenous fractions

Protein is an important constituent of milk which contains about 95% of the total nitrogen present. In the current exploration, protein fractions like CP, TP, caseins and whey proteins, NCN and NPN contents showed significant differences (p<0.05) among different milk species. The CP (5.15% [+ or -] 0.06%), TP (4.53% [+ or -] 0.03%), caseins (3.87% [+ or -] 0.04%) and NPN (0.62% [+ or -] 0.02%) contents were relatively higher in sheep milk followed by buffalo and cow milk (Table 2). The highest whey proteins were in the camel (0.80% [+ or -] 0.03%) milk whereas cow milk represented lowest (0.47% [+ or -] 0.01%). Similarly, the casein contents (2.11% [+ or -] 0.02%) were also found lowest in camel milk as compared to other species. Regarding the NPN fraction, no significant variation was noticed between the buffalo and goat milk. The highest r-values (Table 3) were recorded for the correlations between CP and casein in buffalo (r = 0.82), cow (r = 0.88), sheep (r = 0.86) and goat milk (r = 0.98). The CP also showed positive relationship with whey protein in sheep (r = 0.80) and goat (r = 0.98) milk and NCN contents in camel milk (r = 0.84). Surprisingly, CP was negatively correlated with NPN in buffalo milk (-0.75) while positively correlated with cow milk (r = 0.84) and camel milk (r = 0.85). Different factors such as genetics, species/breed, lactation stages, type of diet, udder health and seasonal variations have pronounced influence on protein contents of milk (Pavic et al., 2002). The caseins and whey proteins were positively correlated with the TP in all milk species but higher results were observed for whey protein in cow (r = 0.83) and camel milk (r = 0.75).

Several findings concerning the protein content of buffalo (Han et al., 2007), cow (Ozrenk et al., 2008), goat (Strzalkowska et al., 2009), and camel milk proteins (Shamsia, 2009) have shown harmony with present research work. Similarly, the TP contents of buffalo, cow, sheep and goat milks are in line with the investigations of Pirsi et al. (2000). The findings of previous studies are comparable with the results of current exploration concerning the casein contents of sheep, goat milk (Borkova and Snaselova, 2005), cow milk (Imran et al., 2008) and camel milk (Khaskheli et al., 2005; Shamsia, 2009). Proteins are an important factor affecting the quality of dairy products as the reduction in proteins and casein (a- and p-casein) contents results in poor cheese making properties (Bernabucci et al., 2002). The findings of Borkova and Snasolva (2005) have shown that cow and goat milk contain 0.47% [+ or -] 0.01% and 0.53% [+ or -] 0.02% whey proteins, respectively.

Amino acid profile of casein and whey proteins

The principal milk proteins such as casein and whey proteins constitute a favorable balance of amino acids, comprised of essential and non-essential amino acids in varying concentrations. The present investigation revealed that leucine was the major amino acid in casein while lysine was second among all essential amino acids as shown in Figure 1. Leucine content was found to be highest in cow milk casein (108 [+ or -] 2.30 mg/g) followed by camel (96 [+ or -] 2.20 mg/g) and buffalo (90 [+ or -] 2.40 mg/g) casein. However, minor differences were noticed in the leucine content of whey proteins from all milk species (Figure 2). Leucine plays a distinct role in protein metabolism and the translation initiation pathway of muscle protein synthesis. It is also involved in reversible phosphorylation of proteins that control mRNA binding to the 40S ribosomal subunit (Anthony et al., 2001).

In the current study, high concentration of essential amino acid lysine was found in camel milk casein (67 [+ or -] 2.39 mg/g) and whey proteins (96 [+ or -] 2.20 mg/g). A substantial quantity of valine, isoleucine, threonine and phenylalanine was also observed in both casein and whey proteins. Highest concentration of valine was found in cow casein (54 [+ or -] 1.42 mg/g) and sheep whey proteins (53 [+ or -] 1.30 mg/g). The isoleucine, phenylalanine and histidine amino acids were at a maximum in casein of goat milk. Phenylalanine concentration was higher in camel (57 [+ or -] 1.50 mg/g), sheep (51 [+ or -] 1.39 mg/g) and cow (44 [+ or -] 1.25 mg/g) milk whey proteins. Similarly, Stancheva et al. (2011) reported the highest percentages for leucine (10.09%) followed by lysine (8.40%) and valine (6.73%) among the essential amino acids and the lowest content was determined for methionine in sheep milk. It was reported by Shamsia (2009) that camel milk proteins possess a high content of essential amino acids except threonine and valine. The lysine and threonine are limiting amino acids in various protein resources. These are strictly indispensable, sensitive to catabolism and important for protein synthesis. Importantly, the amino acid profile differences in dietary proteins also influence their utilization in body. Milk proteins specifically elicited a greater increase in BCAAs (26%) concentrations in peripheral tissues compared to soy protein (Bos et al., 2000; Fouillet et al., 2002). Furthermore, the BCAAs play significant role in weight control via glucose homeostasis and lipid metabolism.

Among the non-essential amino acids, the glutamic acid content was highest in both casein and whey proteins (Figure 3). However, the buffalo (367 [+ or -] 4.50 mg/g) and goat (359 [+ or -] 5.29 mg/g) whey proteins have maximum glutamic acid concentration as compared to casein. The goat casein (144 [+ or -] 3.29 mg/g) and camel whey proteins (129 [+ or -] 4.79 mg/g) represented good content of proline. Cysteine was also observed in casein and whey proteins with minute differences among all milk species. Asparagine and serine was found high in buffalo milk whey proteins as compared to other species under observation (Figure 4). Camel whey proteins indicated higher content of alanine and tyrosine. Previous investigations on amino acid profde of goat milk (Salem et al., 2009) and camel milk (Shamsia, 2009) also depicted that leucine and glutamic acid were the major amino acid in whole casein, while methionine and glycine were present in traces. Similarly, Stancheva et al. (2011) reported highest percentage of glutamic acid (19.08%) followed by proline (10.63%) and aspartic acid (7.27%). Whey protein and amino acid supplements are potential means to enhance lean body mass. Moreover, sulfur containing amino acids (methionine, cysteine) boost up the immune functions through intracellular conversion to glutathione, thereby serves as antioxidants (Hall et al., 2003). These proteins are the subject of great attention for specific dietary manipulations that aim to enhance host defenses.

CONCLUSION

It is concluded that milk composition and nitrogen characterization differ greatly among all milk species under investigation. Moreover, favorable balance of all the essential amino acids, especially, branched-chain amino acids (luecine, isoleucin, and valine) were found in both casein and whey proteins. The present investigation would be useful for the dairy processing industries to formulate nutritionally enhanced milk based functional products for vulnerable segment of population, even from the milk of non-bovine species.

Submitted May 23, 2015; Revised Aug. 19, 2015; Accepted Oct. 3, 2015

http://dx.doi.org/10.5713/ajas.15.0452

CONFLICT OF INTEREST

We certify that there is no conflict of interest with any financial organization regarding the material discussed in the manuscript.

REFERENCES

Ahmad, S., I. Gaucher, F. Rousseau, E. Beaucher, M. Piot, J. F. Grongnet, and F. Gaucheron. 2008. Effects of acidification on physico-chemical characteristics of buffalo milk: A comparison with cow's milk. Food Chem. 106:11-17.

Al Haj, O. A. and H. A. Al Kanhal. 2010. Compositional, technological and nutritional aspects of dromedary camel milk. Int. Dairy! 20:811-821.

Anthony, J. C., T. G. Anthony, S. R. Kimball, and F. S. Jefferson. 2001. Signaling pathways involved in translational control of protein synthesis in skeletal muscle by leucine. J. Nutr. 131:856-860.

AOAC. 2005. Official Methods of Analysis of AOAC International 18th edn., Association of Official Analytical Chemists, Gaithersburg, MD, USA.

Bemabucci, U. N., N. Facetera, B. Ronchi, and A. Nardone. 2002. Effects of the hot season on milk protein fractions in Holstein cows. Anim. Res. 51:25-33.

Borkova, M. and J. Snaselova. 2005. Possibilities of different milk detection in milk and dairy products--A review. Czech J. Food Sci. 23:41-50.

Bos, C., C. Gaudichon, and D. Tome. 2000. Nutritional and physiological criteria in the assessment of milk protein quality for humans. J. Am. Coll. Nutr. 19:191-205.

David, P 1976. The chemical analysis of foods. 7thedn. Churchill Fivingston, Fondon, UK.

Fouillet, H., F. Mariotti, C. Gaudichon, C. Bos, and D. Tome. 2002. Peripheral and splanchnic metabolism of dietary nitrogen are differently affected by the protein source in humans as assessed by compartmental modeling. J. Nutr. 132:125-133.

Fox, P. F., T. P. Guinee, T. M. Cogan, and P. F. H. McSweeney. 2000. Fundamentals of Cheese Science. Aspen Publishers, Inc. Gaithersburg, MD, USA.

GOP (Government of Pakistan). 2014-15. Pakistan Economic Survey. Economic Advisor's Wing, Finance Division, Islamabad, Pakistan.

Ha, E. and M. B. Zemel. 2003. Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people. J. Nutr. Biochem. 14:251-258.

Hall, W. F., D. J. Millward, S. J. Fong, and F. M. Morgan. 2003. Casein and whey exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite. Br. J. Nutr. 89:239-248.

Han, B. Z., Y. Meng, M. Li, Y. X. Yang, F. Z. Ren, Q. K. Zeng, and M. J. Robert Nout. 2007. A survey on the microbiological and chemical composition of buffalo milk in China. Food Control 18:742-746.

IDF (International Dairy Federation). 1993. Determination of milk nitrogen content. 4. Determination of non-protein nitrogen. International Standard FIL-IDF 20B.

Imran, M., H. Khan, S. S. Hassan, and R. Khan. 2008. Physicochemical characteristics of various milk samples available in Pakistan. J. Zhejiang Univ. Sci. 9:546-551.

Khaskheli, M., M. A. Arain, S. Chaudhry, A. H. Soomro, and T. A. Qureshi. 2005. Physico-chemical quality of camel milk. J. Agric. Soc. Sci. 1:164-166.

Kittivachra, R. R., R. Sanguandeekul R. Sakulbumrungsil, and P. Phongphanphanee. 2007. Factors affecting lactose quantity in raw milk. Songklanakarin J. Sci. Technol. 29:937-943.

Mal, G, S. D. Suchitra, and M. S. Sahani. 2007. Changes in chemical and macro-minerals content of dromedary milk during lactation. J. Camel Pract. Res. 14:195-197.

Marshall, R. T. 1993. Standard methods for the examination of dairy products 16th edn. American Publication Health Association (APHA), Washington, DC, USA.

Ozrenk, E. and S. S. Inci. 2008. The effect of seasonal variation on the composition of cow milk in Van Province. Pakistan J. Nutr. 7:161-164.

Pavic, V., N. Antunac, B. Mioc, A. Ivankovic, and J. L. Havranek. 2002. Influence of stage of lactation on the chemical composition and physical properties of sheep milk. Czech J. Anim. Sci. 47:80-84.

Pirsi, A., G. Piredda, M. Corona, M. Pes, S. Pintus, and A. Ledda. 2000. Influence of somatic cell count in ewe's milk composition, cheese yield and cheese quality. In: Proceeding of the 6th great lakes, Dairy Sheep Symposium, Guelph, Canada. pp. 47-59.

Salem, S. A., E. I. El-Agamy, F. A. Salama, and N. H. AbuSoliman. 2009. Isolation, molecular and biochemical characterization of goat milk casein and its fractions. Trop. Subtrop. Agroecosyst. 11:29-35.

Schaafsma, G. 2000. The protein digestibility-corrected amino acid score. J. Nutr. 130:1865- 1867.

Schuster, R. 1988. Determination of amino acids in biological, pharmaceutical, plant and food samples by automated precolumn derivatization and high-performance liquid chromatography. J. Chromatogr. 431:271-284.

Shamsia, S. M. 2009. Nutritional and therapeutic properties of camel and human milks. Int. J. Genet. Mol. Biol. 1:52-58.

Stancheva, N. N. Nay denova, and G Staikova. 2011. Physicochemical composition, properties, and technological characteristics of sheep milk from the Bulgarian dairy synthetic population. Macedonian J. Anim. Sci. 1:73-76.

Steel, R. G. D., J. H. Torrie, and D. A. Dickey. 1997. Principles and Procedures of Statistics. A Bio-Metrical Approach 3rd Ed. McGraw Hill Book Co. Inc., New York, NY, USA.

Strzalkowska, N., A. Jozwik, E. Bagnicka, J. Krzyzewski, K. Horbanczuk, B. Pyzel, and J. O. Horbanczuk. 2009. Chemical composition, physical traits and fatty acid profile of goat milk as related to the stage of lactation. Anim. Sci. Pap. Rep. 27:311-320.

Uallah, S., T. Ahmad, M. Q. Bilal, Zia-ur-Rahman, and G. Muhammad. 2005. The effect of severity of mastitis on protein and fat contents of buffalo milk. Pak. Vet. J. 25:1-4.

Saima Rafiq, Nuzhat Huma, Imran Pasha, Aysha Sameen, Omer Mukhtar1, and Muhammad Issa Khan *

National Institute of Food Science and Technology, University of Agriculture, Faisalabad-38040, Pakistan

* Corresponding Author: Muhammad Issa Khan. Tel: +92-3336627448, E-mail: drkhan@uaf.edu.pk

(1) Food and Marine Resources Research Center, Pakistan Council for Scientific and Industrial Research, Karachi-75280, Pakistan.
Table 1. Chemical composition of different milk species

Species               pH                      Acidity (%)

Buffalo     6.66 [+ or -] 0.01 (a)     0.12 [+ or -] 0.01 (a b)
Cow        6.63 [+ or -] 0.02 (a b)     0.13 [+ or -] 0.01 (b)
Sheep       6.64 [+ or -] 0.02 (b)      0.14 [+ or -] 0.01 (a)
Goat        6.49 [+ or -] 0.05 (d)     0.12 [+ or -] 0.02 (a b)
Camel       6.54 [+ or -] 0.04 (c)     0.12 [+ or -] 0.02 (a b)

Species             Ash (%)                    Fat (%)

Buffalo    0.82 [+ or -] 0.02 (a b)     6.58 [+ or -] 0.02 (b)
Cow         0.72 [+ or -] 0.01 (d)      4.17 [+ or -] 0.03 (d)
Sheep       0.85 [+ or -] 0.01 (a)      6.82 [+ or -] 0.04 (a)
Goat       0.82 [+ or -] 0.02 (a b)     4.61 [+ or -] 0.02 (c)
Camel       0.79 [+ or -] 0.02 (c)      3.11 [+ or -] 0.03 (e)

Species            SNF (%)                   TS (%)

Buffalo    10.09 [+ or -] 0.03 (b)   16.67 [+ or -] 0.03 (b)
Cow        9.13 [+ or -] 0.02 (c)    13.32 [+ or -] 0.04 (d)
Sheep      11.24 [+ or -] 0.02 (a)   18.05 [+ or -] 0.05 (a)
Goat       8.95 [+ or -] 0.04 (d)    13.56 [+ or -] 0.03 (c)
Camel      8.15 [+ or -] 0.05 (e)    11.26 [+ or -] 0.04 (e)

SNF, solid-not-fat; TS, total solids; SD, standard deviation.

All values are mean [+ or -] SD which represent data average of six
samples, each analyzed in triplicate.

(a,b) Values with the same letters within a row or column indicate that
samples do not differ significantly at a significance level of 5%.

Table 2. Milk protein fractions of different milk species

Species            CP (%)                    TP (%)

Buffalo    4.25 [+ or -] 0.07 (b)    3.87 [+ or -] 0.02 (b)
Cow        3.57 [+ or -] 0.03 (c)    3.25 [+ or -] 0.03 (c)
Sheep      5.15 [+ or -] 0.06 (a)    4.53 [+ or -] 0.03 (a)
Goat       3.35 [+ or -] 0.02 (d)    2.95 [+ or -] 0.02 (d)
Camel      3.24 [+ or -] 0.04 (e)    2.89 [+ or -] 0.02 (e)

Species          Casein (%)                 WP (%)

Buffalo    3.20 [+ or -] 0.03 (b)   0.68 [+ or -] 0.02 (b)
Cow        2.79 [+ or -] 0.02 (c)   0.47 [+ or -] 0.01 (e)
Sheep      3.87 [+ or -] 0.04 (a)   0.66 [+ or -] 0.02 (c)
Goat       2.44 [+ or -] 0.03 (d)   0.53 [+ or -] 0.02 (d)
Camel      2.11 [+ or -] 0.02 (e)   0.80 [+ or -] 0.03 (a)

Species           NCN (%)                   NPN (%)

Buffalo    1.05 [+ or -] 0.02 (c)   0.38 [+ or -] 0.02b (c)
Cow        0.77 [+ or -] 0.02 (e)    0.33 [+ or -] 0.03 (d)
Sheep      1.28 [+ or -] 0.03 (a)    0.62 [+ or -] 0.02 (a)
Goat       0.94 [+ or -] 0.01 (d)    0.39 [+ or -] 0.01 (b)
Camel      1.13 [+ or -] 0.02 (b)   0.36 [+ or -] 0.02b (c)

CP, crude protein; TP, true protein; WP, whey proteins; NCN,
non-casein nitrogen; NPN, non--protein nitrogen; SD, standard
deviation. All values are mean [+ or -] SD, representing data average
of six samples, each analyzed in triplicate.

(a, b) Values with the same letters within a row or column indicate
that samples do not differ significantly at a significance level of
5%.

Table 3. Correlation between nitrogen fractions of milk from different
species

                    Buffalo milk                    Cow milk

        CP      TP      CN      WP      CP      TP      CN      WP

TP     -0.77                           0.45
CN     0.82    0.02                    0.88    0.35
WP     0.60    0.25    0.25            0.12    0.83    0.23
NCN    0.41    0.30    0.67    0.45    0.31    0.84    0.10    0.76
NPN    -0.75   -0.15   -0.37   -0.86   0.84    0.37    0.81    -0.04

                    Sheep milk                      Goat milk

        CP      TP      CN      WP      CP      TP      CN      WP

TP     0.47                            0.25
CN     0.86    0.66                    0.98    0.24
WP     0.80    0.43    0.65            0.98    0.25    0.88
NCN    0.50    0.81    0.85    0.35    0.54    0.25    0.59    0.54
NPN    0.36    0.82    0.71    0.20    -0.32   -0.32   -0.44   -0.32

                    Camel milk

        CP      TP      CN      WP

TP     0.54
CN     0.47     0.7
WP     0.15    0.75    0.80
NCN    0.84    0.57    0.77    0.42
NPN    0.85    0.58    0.78    0.41

CP, crude protein; TP, true proteins; CN, casein; WP, whey proteins;
NCN, non casein nitrogen; NPN, non-protein nitrogen.

Correlation between nitrogen fractions was expressed as r.

Figure 1. Essential amino acids content in caseins of
different milk species.

Amino acid concentration (mg/g)

buffalo      cow         goat       sheep       camel

THR, 40    THR, 40     THR, 23     THR, 40     THR, 34

VAL, 49    VAL, 54     VAL, 49     VAL, 49     VAL, 50

MET, 17    MET, 21     MET, 19     MET, 17     MET, 23

ILE, 34    ILE, 60     ILE, 62     ILE, 44     ILE, 34

LEU, 90    LEU, 108    LEU, 69     LEU, 79     LEU, 98

PHE, 49    PHE, 49     PHE, 56     PHE, 45     PHE, 45

HIS, 19    HIS, 29     HIS, 25     HIS, 19     HIS, 19

LYS, 49    LYS, 63     LYS, 61     LYS, 55     LYS, 67

Note: Table made from bar graph.

Figure 2. Essential amino acids in whey proteins of
different milk species.

Amino acid concentration (mg/g)

buffalo      cow         goat       sheep       camel

THR, 38    THR, 41     THR, 31     THR, 30     THR, 25

VAL, 47    VAL, 49     VAL, 47     VAL, 53     VAL, 33

MET, 17    MET, 22     MET, 22     MET, 25     MET, 27

ILE, 39    ILE, 34     ILE, 35     ILE, 25     ILE, 29

LEU, 74    LEU, 81     LEU, 71     LEU, 81     LEU, 83

PHE, 38    PHE, 44     PHE, 39     PHE, 51     PHE, 57

HIS, 15    HIS, 16     HIS, 16     HIS, 18     HIS, 23

LYS, 53    LYS, 65     LYS, 63     LYS, 71     LYS, 96

Note: Table made from bar graph.

Figure 3. Non-Essential amino acids profile in caseins of
different milk species.

Amino acid concentration (mg/g)

buffalo       cow         goat       sheep       camel

ASP, 66     ASP, 62     ASP, 38     ASP, 65     ASP, 61

SER, 50     SER, 47     SER, 39     SER, 50     SER, 44

GLU, 254    GLU, 218    GLU, 241    GLU, 338    GLU, 303

PRO, 57     PRO, 96     PRO, 144    PRO, 55     PRO, 73

GLY, 15     GLY, 12     GLY, 15     GLY, 14     GLY, 14

ALA, 22     ALA, 21     ALA, 28     ALA, 21     ALA, 25

CYS, 8      CYS, 12     CYS, 10     CYS, 8      CYS, 13

TYR, 51     TYR, 56     TYR, 65     TYR, 49     TYR, 59

ARG, 112    ARG, 40     ARG, 36     ARG, 32     ARG, 28

Note: Table made from bar graph.

Figure 4. Non-Essential amino acids in whey proteins of
different milk species.

amino acid concentration (mg/g)

buffalo       cow         goat       sheep       camel

ASP, 74     ASP, 65     ASP, 70     ASP, 5      ASP, 36

SER, 52     SER, 47     SER, 51     SER, 46     SER, 36

GLU, 367    GLU, 350    GLU, 359    GLU, 318    GLU, 257

PRO, 77     PRO, 69     PRO, 67     PRO, 102    PRO, 129

GLY, 15     GLY, 11     GLY, 14     GLY, 12     GLY, 12

ALA, 22     ALA, 20     ALA, 24     ALA, 35     ALA, 39

CYS, 9      CYS, 12     CYS, 12     CYS, 13     CYS, 16

TYR, 44     TYR, 43     TYR, 42     TYR, 45     TYR, 58

ARG, 8      ARG, 10     ARG, 7      ARG, 5      ARG, 5

Note: Table made from bar graph.
COPYRIGHT 2016 Asian - Australasian Association of Animal Production Societies
No portion of this article can be reproduced without the express written permission from the copyright holder.
Copyright 2016 Gale, Cengage Learning. All rights reserved.

Article Details
Printer friendly Cite/link Email Feedback
Author:Rafiq, Saima; Huma, Nuzhat; Pasha, Imran; Sameen, Aysha; Mukhtar, Omer; Khan, Muhammad Issa
Publication:Asian - Australasian Journal of Animal Sciences
Article Type:Report
Date:Jul 1, 2016
Words:4767
Previous Article:Evaluation of Salmonella growth at low concentrations of NaN[O.sub.2] and NaCl in processed meat products using probabilistic model.
Next Article:Estimation of sensory pork loin tenderness using Warner-Bratzler shear force and texture profile analysis measurements.
Topics:

Terms of use | Privacy policy | Copyright © 2019 Farlex, Inc. | Feedback | For webmasters