Whey lactoferrin

Lactoferrin (from human whey). Purified by direct adsorption on cellulose phosphate by batch extraction, then eluted by a stepped salt and pH gradient. [Foley and Bates Anal Biochem 162 296 1987.]... 

Lactoferrin is the major whey protein present in breast milk (Teraguchi et ah, 1996) with many microbicidal properties (Leon-Sicairos et ah, 2006). The concentration of lactoferrin in milk has been reported as 1 g/liter in mature milk and 7 g/liter in colostrum (Houghton et ah, 1985). The concentration of lactoferrin in breast milk is controlled by the reproductive hormones prolactin and estrogen (Ward et ah, 2005). Lactoferrin has been demonstrated to resist digestion in the infant gut as it has been recovered intact from the stool of breast-fed infants (Bemt and Walker, 1999). Lactoferrin acts mainly in an iron-free state (apo-lactoferrin) and its microbicidal activity is reported to increase in proportion to its concentration in milk (Leon-Sicairos et ah, 2006). 

Butler, J. E. 1973. The occurrence of immunoglobulin fragments, two types of lactoferrin and a lactoferrin-IgG2 complex in bovine colostral and milk whey. Biochim. Bio-phys. Acta 295, 341-351. 

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-... 

Chiu, C.K. and Etzel, M.R. 1997. Fractionation of lactoperoxidase and lactoferrin from bovine whey using a cation exchange membrane. J. Food Sci. 62(5), 996-1000. 

Uchida, T., Sato, K., Kawasaki, Y., and Dosako, S. 1996. Separation of lactoperoxidase, secretory component and lactoferrin from milk or whey with a cation exchange resin. US Patent No. 5,516,675. 

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. 

Lactoferrin, lactotransferrin. Important component of the human milk bacteriostatic system also found in human and bovine tear proteins. Isoln from human whey by a single chromatographic step L. Blackberg, O. Hernell, FEES... 

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

Contrary to other whey proteins, a Fe " ion is present in lactoferrin molecule [3]. Similarly to immunoglobulins, it has the antimicrobial character [46]. Whey is appropriate for extraction of lactoferrin and cation-exchange chromatography is proposed for its purihcation. Heat treatment at pH 4.0 does not denature the protein therefore, this pH is suitable for its pasteurization. Recently, some beneficial aspects of lactoferrin on human s health have been regarded. Its exceptional properties such as antiinfective, anticancer, antioxidant and antimicrobial activities enhance its utility in pharmaceutical and food industries. Remarkably, lower pH values (2-3) enhance its antibacterial activity. The results of clinical studies about positive effects of lactoferrin on human and animals health have been published [49]. 

Glycoproteins, bovine whey. See Glycoproteins Glycoproteins, iron-binding, milk, lactoferrin. See Lactoferrin Glycosaminoglycans... 

Lacto-serum. See Whey Lactosum. See Lactose Lactotransferrin. See Lactoferrin Lactoyl methylsilanol elastinate... 

Although the use of CE in food analysis is limited compared with LC, many applications have been reported in recent years in the study of food proteins and peptides. It has been shown that the sensitivity provided by CE using LIE detection for bovine whey proteins is twice as good as that provided by UV detection, under the same separation conditions. LIF detection has also been used together with affinity interactions to enhance the detection sensitivity in CE. For instance, an immunoassay detection method has been described using a polyclonal antibody marked with fluorescein to determine lactoferrin. CE-LIF has also been applied to the determination of amines and amino acids in several samples such as wine and milk products. 

Milk proteins soluble proteins present in milk, consisting of caseins and whey proteins. The chief caseins are a, p and K-casein. The most important whey proteins are p-Iactoglobulin, a-lactalbumin and lactoferrin. In addition, milk contains several enzyme proteins, e.g. lactoperoxidase, xanthine oxidase and immunoglobulins. IgG, IgA and IgM. These immunoglobulins are absorbed directly and without cleavage by the intestine of the infant, and provide it with passive immtmity against those pathogens to which the mother is immune. 

Iron supplementation to meet nutritional requirements can seriously limit the shelf life of milk products especially infant formulas. lipid oxidation can be controlled in iron-supplemented milk by using lactoferrin, a non-heme ironbinding glycoprotein found in human (1.4 mg/ml) and bovine milk (0.1 mg/ ml). Lactoferrin in bovine milk is 22% saturated with iron compared to 4% in mature human milk. Compared to human milk, infant formulas are more susceptible to lipid oxidation because they are supplemented with greater amounts of iron and do not contain lactoferrin. This antioxidant protein in milk has an important activity by binding prooxidant iron ions. Commercially available bovine lactoferrin, isolated from cheese whey, inhibited lipid... 

Lampreave F, Pineiro A, Brock JFI et al (1990) Interaction of bovine lactoferrin with other proteins of milk whey. Int J Biol Macromol 12(l) 2-5... 

Law, B. A, and Reiter, B, (1977) The isolation and bacteriostatic properties of lactoferrin from bovine milk whey. 

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. 

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