Beta-casein

Nylander T and Wahlgren N M 1997 Forces between adsorbed layers of beta-casein Langmuir 6219-25... 

The increased hydration at low temperature is due to lower protein content in the pellet owing to dissociation of protein from the micelle (mainly beta-casein), and corresponds to data from the literature42. 

Muller-Renaud, S.P., Dupont, D., and Delie, P. 2004. Quantification of beta-casein in milk and cheese using an optical immunosensor. J Agric Food Chem 52 659-664. 

Creamer, L.K. and Richardson, T. 1984. Anomalous behavior of bovine alpha si- and beta-caseins on gel electrophoresis in sodium dodecyl sulfate buffers. Arch Biochem Biophys 234(2) 476M-86. 

Righetti, P.G., Nembri, F., Bossi, A., and Mortarino, M. 1997. Continuous enzymatic hydrolysis of beta-casein and isoelectric collection of some of the biologically active peptides in an electric field. Biotechnol. Prog. 13, 258—264. 

Creamer, L.K. 1971. Beta-casein hydrolysis in Cheddar cheese ripening. N.Z. J. Dairy Sci. Technol. 6, 91. 

Sausse, R, Aguie-Beghin, V., Douillard, R. (2003). Effects of epigallocatechin gallate on beta-casein adsorption at the air/water inieTlace.Langmuir, 19, Ihl—lAh. 

Yan SB, Wold F. Neoglycoproteins in vitro introduction of glycosyl units at glutamines in beta-casein using transglutaminase. 52. Biochemistry 1984 23 3759-3765. 

S.-L. Wu, J. Kim, W.S. Hancock, B. Karger, Extended range proteomic analysis (ERPA) A new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive PTM-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGER), J. Proteome Res., 4 (2005) 1155. 

Darewicz, M., and Dziuba, J. (2001). The effect of glycosylation on emulsifying and structural properties of bovine beta-casein. Nahrung 45, 15-20. 

Bieck, G.T., Choi, B.K., Wheeler, M.W., and Jimenez-Flores, R. (1998a). Modification of bovine beta-casein to improve the characteristics and manufacturing properties of cow s milk. wv ctraill.uiuc.edu/dairynet/paperDisplay ContentID = 245. 

Chong, D.K., et al.. Expression of the human milk protein beta-casein in transgenic potato plants. Transgenic Res, 1997 6(4) 289-296. 

The predominant protein in goat milk is beta casein (10-20 mg mL ) this is thought to comprise 25-50% of the total protein ( 30mgmL ). The beta casein... 

Fig. n.3 Schematic representation of the BC5 transgene for recombinant expression of rhAT in the miik of transgenic animais. The cDNA encoding hAT (striped box) repiaces the coding region of the caprine beta-casein gene. This cDNA is... 

The applications of foam fractionation are many. Its use is primarily to concentrate materials present in low concentration (as low as 10 " M/L) in liquids where other processes are not economical. On a commercial scale, this process is used to treat waste water to remove organic waste material and to remove ions from process streams such as the oxyanions of Re(VIII), Mo(VI), Cr(VI), W(VI) and V(V) and the cyanide complex anions or the chloride complexes of Zn(Il), Cd(II), Hg(II), and Au(Ill). In the laboratory, it is used to concentrate proteins such as bovine albumin, cytochrome-c, barley malt, alpha amalyase, and beta casein, as well as proteins and enzymes from various plant and animal systems. 

The major casein components differ in their behavior toward the calcium ion (145). The aB group of caseins are very susceptible to precipitation by the calcium ion. Beta casein undergoes a temperature-dependent precipitation in the presence of calcium ion, being soluble at 4°C and insoluble at 35°C. -Casein, discovered by Waugh and von Hippel (146) in 1956, is resistant to precipitation in the presence of calcium ion, and when mixed with appropriate portions of s- and -casein, it forms complexes or micelles with these caseins and stabilizes... 

FIGURE 9.4 A comparison of amino acid recoveries after hydrolysis using microwave-mediated hydrolysis and conventional hydrolysis methods for the protein beta-casein. (Reproduced with permission from Sandoval, W. N. Pham, V. C. Lill, J. R. Drug Discov. Today 2008,13, 1075-1081. Copyright Elsevier.)... 

PHILIP, R DARNOWSKI, D.W., MAUGHAN, P.J., VODKIN, L.O., Processing and localization of bovine beta-casein expressed in transgenic soybean seeds under control of a soybean lectin expression cassette, Plant Sci., 2001,161, 323-335. 

Detection of phosphorylated proteins and peptides can be enhanced by selectively isolating these species. Online immobilized metal affinity chromatography (IMAC)-CE-ESI-MS is such a powerful analytical tool. The IMAC resin retains and preconcentrates phosphorylated proteins and peptides, CE separates the phosphorylated species and MS/MS identifies the components and their phosphorylation sites. Cao and Stults applied this method to the analysis of phosphorylated angiotensin II and tryptic digests of a- and /3-casein (CE conditions buffer, 0.1% acetic acid/10% methanol uncoated capillary). Beta-casein is a well-characterized protein with five phosphorylation sites and is widely used as a standard for protein phosphorylation studies. 

Forrest, S. A. Yada, R. Y Rousseau, D., Interactions of vitamin D-3 with bovine beta-lactoglobulin A and beta-casein. Journal of Agricultural and Food Chemistry (2005) 53, 8003-8009. 

Kroening, T.A. Mukeiji, P. Hards, R.G. Analysis of beta-casein and its phosphoforms in human milk. Nutr. Res. 1998,18, 1175-1186. 

Livney YD, Schwan AL, Dalgleish DG (2004) A study of beta-casein tertiary structure by intramolecular crosslinking and mass spectrometry. J Dairy Sci 87 3638-3647... 

S2- and beta-casein cDNAs comparisons with related sequences in other species. MoJ. Biol. Evol., 4, 231 241. 

Blackburn, D.E., Hobbs, A.A., and Rosen, J.M. (1982) Rat beta casein cDNA sequence analysis and evolutionary comparisons. Nudeic Acids Res.,... 

Bonsing, )., Ring, J.M., Stewart, A.F., and Mackinlay, A.G. (1988) Complete nucleotide sequence of the bovine beta-casein gene. Aust. J. Biol. Sd., 41, 527-537. 

Jiminez-Flores, R., Klang, Y.C., and Richardson, T. (1987) Cloning and sequence analysis of bovine beta-casein cDNA. Biochem. Biophys. Res. Commun., 142, 617-621. 

M.L., and Houdebine, L.M. (1991) The structure of the gene encoding rabbit beta-casein. Gene, 97, 301-306. 

Liu M, Damodaran S. Effect of transglutaminase-catalyzed polymerization of beta-casein on its emulsifying properties. 7 A ric Food Chem. 47 (4) 1514-1519,1999. 

Caessens PW, Gruppen H, Slangen CJ, Visser S, Voragen AG. Functionality of beta-casein peptides Importance of amphipathicity for emulsion-stabilizing properties. J Agric Food Chem. 47 (5) 1856-1862,1999. 

Foam fractionation is a relatively inexpensive technique for protein separation. Most studies in the literature are, however, experimental and very few report on industrial appUcations. Among other appUcations, foam liaclionation has been used to separate wheat flour proteins, ovalbumin, lysozyme, egg albumin, milk proteins (e.g., beta-casein, bovine lactoferrin, bovine serum albumin, alpha-lactalbumin, and beta-lactoglobulin) and potato protein from potato juice waste water after starch extraction (Weijenberg et al., 1978 Keller et al., 1997 Hossain and Fenton, 1998 Brown et al., 1999 Wang and Liu, 2(X)3 Wang etal., 2009). 

Gas flow requirements to produce stable foams were found to be lower for bovine serum albumin and beta-lactoglobulin, which had greater surface activity compared to beta-casein and alpha-lactalbumin, and the enrichment factor and percentage volume loss in foam were also higher for the former proteins (Hossain and Fenton, 1998). 

Sandrd, C., Gleizes, A., Eorestier, F., et al. (2001) A peptide derived from bovine beta-casein modulates functional properties of bone marrow-derived macrophages from germfree and human flora-associated mice. J Nutr 131,... 

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