Lactoferrin 3-lactoglobulin

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-... 

It is interesting to note that /3-lactoglobulin is the major protein in cow s milk whey, but it is absent from human milk whey. However, the content of a-lactoalbumin and immunoglobulins (Ig) is higher in human than in cow s milk whey. Serum albumin and lactoferrins are found in similar concentrations in human and cow s milk whey, and the amount of lactoferrin is higher in colostrum than in mature milk. In any case, lactoferrin is present in milk throughout the lactation period. 

Whey proteins are consisted of ]S-lactoglobulin, a-lactalbumin, proteose peptone, serum albumin, immunoglobulins and lactoferrin. In contrast with caseins, they are... 

In this section, a brief overview of the structural characteristics of the food proteins most widely used in studies on protein-protein complex formation is presented. Proteins presented below and in Table 1 are from milk [p-lactoglobulin (P-Lg), a-lactalbumin (a-La), bovine serum albumin (BSA), lactoferrin, caseins] or egg white (ovalbumin, lysozyme), even if proteins from other sources (including gelatin and soy and wheat proteins) are also used for self-assemblies and complex formation studies. The proteins presented are mainly monomers, but are able to self-assemble into oligomers or aggregates in some specific conditions. These conditions are also addressed. 

P-Lactoglobulin Apo a-lactalbumin Lysozyme Lactoferrin aggregates (nnpnblished data)... 

Selective elution, also known as ion exchange chromatography, is the process most often used to make whey protein isolates. Using selective elution, whey protein solution is applied to an ion exchange column so that all of the proteins bind to the column. The column is then rinsed and the individual proteins are eluded one by one to produce highly purified whey proteins. This process can be used to both concentrate and fractionate the proteins. If done carefully, the native protein structures can be retained. However, some of the smaller peptides such as lactoferrin may have a decreased concentration, while the P-lactoglobulin protein fraction tends to increase in whey protein isolates. 

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). 

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