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Bovine milk proteins

Table 5.8 Some physicochemical properties of the major (bovine) milk proteins... Table 5.8 Some physicochemical properties of the major (bovine) milk proteins...
Saz and Marina [148] published a comprehensive review on HPLC methods and their developments to characterize soybean proteins and to analyze soybean proteins in meals. In the case of soybean derived products, a number of papers dealing with cultivar identification [149,150], quantification of soybean proteins [151-154], detection of adulteration with bovine milk proteins [151,155-158], and characterization of commercial soybean products on the basis of their chromatographic protein profile [159,160] have been published in the last years. Other studies deal with the analysis of soybean proteins added to meat [161-165], dairy [151,165-167], and bakery products [156,163,168,169]. The same research group developed perfusion RP-HPLC methods for very rapid separation of maize proteins (3.4 min) and characterization of commercial maize products using multivariate analysis [170], and for the characterization of European and North American inbred and hybrid maize lines [171]. [Pg.580]

Identification and quantification of Milk Centrifugation at 4°C (for skimming) major bovine milk proteins in milk samples... [Pg.581]

In contrast, the whey proteins are relatively small globular proteins. a-Lactalbumin represents about 20 % of the protein content of bovine whey (3.5 % of total bovine milk protein), and it is the principal protein in human milk (Brew and Grobler, 1992). Nanotube assembly has been discovered in some solutions containing a hydrolysed derivative of this protein. And it appears that the a-lactalbumin nanotube is unique in the sense that it is the only artificial nanotube that has so far been made from a food protein (Graveland-Bikker et al., 2004 Graveland-Bikker and de Kruif, 2006). As for p-lactoglobulin, it has the capacity under certain specific conditions to form nano-fibres in aqueous media (as can various other globular food proteins, such as ovalbumin, soy proteins, and bovine serum albumin) (van der Linden, 2006 Nicolai, 2007). [Pg.157]

The use of HPLC for the analysis of bovine milk proteins was introduced by Diosady et al. (59), who compared SE-HPLC on two SynChropac GPC-100 columns in series and RP-HPLC on a lO-jUm-particle-sizc RP-8 column, both with UV detection, for the separation of dialyzed freeze-dried whey proteins. Column temperature was 40°C and 47°C, respectively. Samples were eluted with Tris-buffer pH 6 for SE-HPLC and a linear gradient of two solvents, i.e., 98% 0.5 M KH2P04, pH 2, and 98% isopropanol, each with 2% 2-methoxyethanol for RP-HPLC. They... [Pg.140]

The evolution in separation methods described in the preceding paragraph is focused completely on the separation of bovine milk proteins. Much less information is available on the use of HPLC techniques to separate nonbovine milk proteins. Law and co-workers applied cation-exchange FPLC to the quantitative separation of ovine casein (51) and caprine casein (52) on a Mono S HR 5/5 column, using a 20 mM acetate, 6 M urea, pH 5, and 20 mM acetate, 6 M urea, 1 M NaCl, pH 5 elution buffer system. They observed that ovine and caprine casein contains much less as- and much more /3-casein compared to bovine casein. However, caprine casein contains a higher K-cascin content compared to bovine or ovine casein (52). [Pg.145]

S Visser, CJ Slangen, HS Rollema. Phenotyping of bovine milk proteins by reversed-phase high-performance liquid chromatography. J Chromatogr 548 361-370, 1991. [Pg.163]

One of the most important factors that determine whether or not a protein is usable in the fabrication of a food product is its functionality. The functionality results from a combination of physico-chemical properties that define the behavior of the food protein in food systems. It is evident that a detailed understanding of food protein functionality requires an intimate knowledge of the protein structure. The bovine milk protein system has been studied in great detail. Although providing useful structure-function... [Pg.50]

Pihlanto-Leppala, A., Rokka, T., and Korhonen, H. 1998. Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins. Int. Dairy J. 8, 325-331. [Pg.68]

Kayser, H. and Meisel, H. 1996. Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins. FEBS Lett. 383, 18-20. [Pg.258]

Wong, C.W., Middleton, N., Montgomery, M., Dey, M., and Carr, R.I. 1998a. Immunostimulation of murine spleen sells by materials associated with bovine milk protein fractions. J. Dairy Sci. 81, 1825-1832. [Pg.275]

F. Kjeldsen, K. F. Haselmann, B. A. Budnik, E. S. Sorensen, and R. A. Zubarev, Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage, Anal. Chem., 75 (2003) 2355-2361. [Pg.268]

Amigo, L. Recio, I. Ramos, M. Genetic pol3miorphism of bovine milk proteins Its influence on technological properties of milk—A review. Int. Dairy J. 2000, 10 (3), 135-149. [Pg.1735]

Proteolytic hydrolysates are increasingly used with patients suffering from protein hypersensitivity. Both the first-generation hydrolysates of casein and the second generation whey protein hydrolysates are highly hydrolyzed. Recently, third generation, less degraded, whey protein hydrolysates have been described [122]. Infant formulas based on cow s milk protein have been widely used as supplements or substitutes [180]. However, bovine milk proteins... [Pg.159]

Rehder-Silinski, M. A., McGown, L. B. (2003). Capillary electrochromatographic separation of bovine milk proteins using a G-quartet DNA stationary phase. J Chromatogr A 1008, 233-245. [Pg.296]

Andrews, A.T. Taylor, M.D. Owen, A.J. Rapid analysis of bovine milk proteins by fast protein liquid chromatography. J. Chromatogr. 1985, 348,177-185. [Pg.1511]

Table 10.8. Amino acid sequences of bovine milk proteins... Table 10.8. Amino acid sequences of bovine milk proteins...
Mahe, S., Messing, B., Thuillier, E, and Tome, D. (1991). Digestion of bovine milk proteins in patients with a high jejunostomy. Am J Clin Nutr 54 534—538. [Pg.158]

Certain probiotic strains have been shown to stimulate the immune system in a beneficial, non-inflammatory manner. Such strains have also been shown to relieve the symptoms of allergic conditions such as atopic eczema and bovine milk protein intolerance in human feeding studies. The mechanisms underlying such beneficial modulation of immune response have not yet been fully elucidated. [Pg.180]


See other pages where Bovine milk proteins is mentioned: [Pg.101]    [Pg.177]    [Pg.183]    [Pg.229]    [Pg.74]    [Pg.475]    [Pg.58]    [Pg.457]    [Pg.599]    [Pg.861]    [Pg.861]    [Pg.210]    [Pg.224]    [Pg.285]    [Pg.502]    [Pg.400]    [Pg.607]   
See also in sourсe #XX -- [ Pg.114 ]




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