Beta-lactoglobulin

Kontopidis, G., Holt, C., and Sawyer, L. (2004). Invited review Beta-lactoglobulin Binding properties, structure, and function. /. Dairy Sci. 87, 785-796. 

Kuwata, K., Shastry, R., Cheng, H., Hoshino, M., Batt, C. A., Goto, Y., and Roder, H. (2001). Structural and kinetic characterization of early folding events in beta-lactoglobulin. Nat. 

Mousavi, S. H., Bordbar, A. K., and Haertle, T. (2008). Changes in structure and in interactions of heat-treated bovine beta-lactoglobulin. Protein Pept. Lett. 15, 818-825. 

Kobayashi, T., Ikeguchi, M., and Sugai, S. (2000). Molten globule structure of equine beta-lactoglobulin probed by hydrogen exchange./ Mol. Biol. 299, 757-770. 

Kroes-Nijboer A, Lubbersen YS, Venema P, van der Linden E (2009) Thioflavin T fluorescence assay for [beta]-lactoglobulin fibrils hindered by DAPH. J Struct Biol 165(3) 140... 

Uversky, V. N., Narizhneva, N. V., Kirschstein, S. O., Winter, S., and Lober, G. (1997). Conformational transitions provoked by organic solvents in beta-lactoglobulin Can a molten globule like intermediate be induced by the decrease in dielectric constant FoldingDes. 2, 163-172. 

Boye, J.I., A. A. Ismail, and I. Alii. 1996. Effects of physicochemical factors on the secondary structure of beta-lactoglobulin. J Dairy Res 63 97-109. 

Zimet, P., Livney, Y.D. (2009). Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for co-3 polyunsaturated fatty acids. Food Hydrocolloids, 23, 1120-1126. 

Chevalier F, Chobert JM, Dalgalarrondo M, Choiset Y, Haertle T. Maillard glycation of beta-lactoglobulin induces confonnation changes. Nahrung 2002 46(2) 58-63. 

Lactalbumin is an often misused synonym for whey protein. In the supplemental protein industry, lactalbumin is a reference to whey protein that has been manufactured by a heat and acid process. Since heat and acid both denature vital protein fractions (broken a part = denature), and lactalbumin is a high heat process, the product retains few of its original bodybuilding qualities. It also contains above normal levels of beta-lactoglobulin. Biological activity sucks. 

Mother s milk is an often coined term for products that mimic the natural mother s milk contents. Actual human mother s milk contains about 40-50% casein and 50-60% whey, and about 17% lactoferrin with no beta-lactoglobulin. As I said earlier, mother s milk contains alfa lactoglobulin. This is very different from cow s milk which contains about 80% casein and 20% whey with 1% lactoferrin being average. Lactoferrin has anti-viral activity, and is a potent immune system booster. Obviously this is an advantage for new born human (rug rats) since they lack complete immune system functions. Remember the fact that human mother s milk dominant protein fraction is alfa-lactalbumin Well, there is a research project on going which claims acid folded alfa-... 

The simultaneous separation and recovery of acidic and basic bioactive peptides by employing electrodialysis with ultrafiltration membranes has also been investigated recently [30]. This work aims at demonstrate the feasibility of separating peptides from a beta-lactoglobulin hydrolysate, using an ultrafiltration membrane stacked in an electrodialysis cell, and a study of the effect of pH on the migration of basic/ cationic and acid/anionic peptides in the electrodialysis configuration. 

Bovine alpha-lactalbumin Bovine beta-lactoglobulin A and B BSA... 

Inoue, R., Matsushita, S., Kaneko, H., Shinoda, S., Sakaguchi, H., Nishimura, Y. et al. 2001. Identification of beta-lactoglobulin-derived peptides and class IIHLA molecules recognized by T cells from patients with milk allergy. Clin Exp Allergy 31(7) 1126-1134. 

Jarvinen, K.M., Chatchatee, R, Bardina, L., Beyer, K., and Sampson, H.A. 2001. IgE and IgG binding epitopes on alpha-lactalbumin and beta-lactoglobulin in cow s milk allergy. Int Arch Allergy Immunol 126(2) 111—118. 

Ehn, B.M., Ekstrand, B., Bengtsson, U., and Ahlstedt, S. 2004. Modification of IgE binding during heat processing of the cow s milk allergen beta-lactoglobulin. JAgric Food Chem 52(5) 1398-1403. 

Fritsche, R., Adel-Patient, K., Bernard, H., Martin-Paschoud, C., Schwarz, C., Ah-Leung, S., Wal, J.M. 2005. IgE-mediated rat mast cell triggering with tryptic and synthetic peptides of bovine beta-lactoglobulin. Int Arch Allergy Immunol 138 291-297. 

Godovac-Zimmermann, J., Conti, A., Liberatori, J., and Braunitzer, G. 1985. Homology between the primary structures of beta-lactoglobulins and human retinol-binding protein Evidence for a similar biological function Biol Chem Hoppe Seyler 366(4) 431-434. 

Livney, Y.D., Verespej, E., and Dalgleish, D.G. 2003. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin. J Agric Food Chem. 51(27) 8098-8106. 

Selo, I., Clement, G., Bernard, H., Chatel, J.-M., Creminon, C., Peltre, G., and Wal, J.-M. 1999. Allergy to bovine beta lactoglobulin Specificity of human IgE to tryptic peptides. Clin Exp Allergy 29 1055-1063. 

Evidence for a common epitope between bosine Ralpha-lactalbumin and beta-lactoglobulin. Biol Chem 379(12) 1453-1456. 

Mullally, M.M., Meisel, H., and FitzGerald, R.J. 1997. Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine beta-lactoglobulin. FEBS Lett. 402, 99-101. 

Pihlanto-Leppala, A., Paakkari, I., Rinta-Koski, M., and Antila, P. 1997. Bioactive peptide derived from in vitro proteolysis of bovine beta-lactoglobulin and its effect on smooth muscle. J. Dairy Res. 64, 149-155. 

Pihlanto-Leppala, A., Marnila, P., Hubert, L., Rokka, T., Korhonen, H., and Karp, M. 1999. The effect of alpha-lactalbumin and beta-lactoglobulin hydrolysates on the metabolic activity of Escherichia coli JM103. J. Appl. Microbiol. 87, 540-545. 

Sannier, F., Bordenave, S., and Piot, J.M. 2000. Purification of goat beta-lactoglobulin from whey by an ultrafiltration membrane enzymic reactor. J. Dairy Res. 67, 43 -51. 

Manderson, G.A., Creamer, L.K., and Hardman, M.J., Effect of heat treatment on the circular dichroism spectra of bovine beta-lactoglobulin A, B, and C, J. Agric. Food Chem., 47, 4557 1567, 1999. 

Figure 4.13 Anatomy of selected proteins. (A) The /3 subunit of hemoglobin carrying a heme molecule (B) triose isomerase and (C) /3-lactoglobulin carrying a molecule of vitamin A. Spirals represent helix segments, and the broad arrows are pleated sheet polypeptide segments showing the direction from the N to the C terminus. (A and B reproduced with permission from Richardson JS. The anatomy and taxonomy of protein structure. Adv Prot Chem 34 168-339, 1981. C reproduced with permission from Papiz MZ, Sawyer L, Eliopoulos EE, North ACT, Findlay JBC, Sivaprasadarao R, Jones TA, Newcomer ME, Kraulis PJ. The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324 383-385, 1986.)...

Chen, L., and Subirade, M. (2005), Chitosan/beta-lactoglobulin core-shell nanoparticles as nutraceutical carriers, Biomaterials, 26(30), 6041-6053. 

Chatel, J. M., Langella, P, Adel-Patient, K., Commissaire, J., Wal, J. M., and Corthier, G. (2001), Induction of mucosal immune response after intranasal or oral inoculation of mice with Lactococcus lactis producing bovine beta-lactoglobulin, Clin. Diag. Lab. Immunol., 8, 545-551. 

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