P-Lactoglobulin

Godovac-Zimmerman, J. The structural motif of p-lactoglobulin and retinol-binding protein a basic framework for binding and transport of small hydrophobic molecules Trends Biochem. Sci. 

Papiz, M.Z., et al. The structure of p-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324 383-385, 1986. 

Milk Morinaga FASPEK Milk Western Blot Kit ( 3-lactoglobulin) Morinaga Inshtute of Biological Sciences Co. P-lactoglobulin 18,400... 

Gezimati, J., Creamer, L. K., and Singh, H. (1997). Heat-induced interactions and gelation of mixtures of p-lactoglobulin and a-lactalbumin. /. Agric. Food Chem. 45,1130-1136. 

Fig. 3 SDS-PAGE Photograph Separation (Lane Mr and A) and activity staining (Lane B and C) of the crude filtrate of Funalia trogii. Lane Mr standard molecular weight markers ([3-galactosi-dase, 118.0 kDa bovine serum albumin, 79.0 kDa ovalbumin, 47.0 kDa carbonic anhydrase, 33.0 kDa P-lactoglobulin, 25.0 kDa and lysozyme, 19.5 kDa). Relative mobilities of the standard markers vs. common logarithms of their molecular masses were plotted.With the linear regression output, the molecular masses of the proteins in the crude filtrate were estimated (taken from [18])...

High expression levels of proteins are potentially attained. In many instances, the level of expression exceeds 1 g protein/litre milk. In one case, initial expression levels of 60 g l-1 were observed, which stabilized at 35 g L1 as lactation continued (the expression of the arantitrypsin gene, under the influence of the ovine P-lactoglobulin promoter, in a transgenic sheep). Even at expression levels of 1 g L1, one transgenic goat would produce a similar quantity of product in 1 day as would be likely recoverable from a 50-1001 bioreactor system. 

Miller, K., Meredith, C, Selo, I. amd Wal, J-M., Allergy to P-lactoglobulin specificity of immunoglobulin E generated in the Brown Norway rat to tryptic and synthetic peptides. Clin. Exp. Allergy., 29, 1696, 1999. 

Chemical reactions Polymerization of casein and whey proteins are due to some kind of chemical reactions. The different proteins as found in the supernatant of milk after precipitation at pH 4.6 are collectively called whey proteins. These globular proteins are more water soluble than caseins and are subject to heat dena-turation. Denaturation increases their water-binding capacity. The principal fractions are P-lactoglobulin, a-lactalbumin, bovine serum albumin (BSA), and immunoglobulins (Ig). 

Detection of p-lactoglobulin modification in milk samples as a consequence of heat treatments Detection of p-lactoglobulins as a marker to detect fraudulent addition of bovine milk during manufacturing of buffalo Mozzarella... 

Hernandez-Ledesma, B., D avalos, A., Bartolom e, B., and Amigo, L. (2005). Preparation of antioxidant enzymatic hydrolysates from a-lactalbumin and p-lactoglobulin. Identification of active peptides by HPLC-MSMS. ]. Agric. Food Chem. 53,588-593. 

Figure 1.2 TEM micrographs of p-lactoglobulin at pH = 2 after heating at 80 °C for 10 h (image A) after pH was then adjusted to pH = 7 (image B) or pH = 8 (image C). Reproduced front Veerman el al. (2003) with permission.

McClements, 2006 Anal et al., 2008). Different combinations of proteins and polysaccharides (e.g., P-lactoglobulin + pectin, carrageenan or alginate casein + pectin) have been investigated within the context of multilayer emulsion stabilization (Guzey and McClements, 2006). It seems that the main technical challenge associated with the utilization such complex formation for layer-by-layer emulsion stabilization is the avoidance of bridging flocculation (McClements, 2005, 2006). 

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