This report reviews the nomenclature of the milk proteins of cow's milk in light of more recent advances in our knowledge. With the establishment of the primary structures of a number of these proteins, we now have a definite identification of alphas1-, kappa-, beta-, and the gamma-caseins as well as beta-lactoglobulin and alpha-lactalbumin. On the basis of new information on their primary structures and relationship to beta-casein polymorphs, changes in nomenclature have been recommended for proteins of the gamma-casein fraction. Although the primary structure serves as the unambiguous definition of proteins for which it is known, a more practical identification is necessary. We recommend that their behavior in gel electrophoresis under suitable conditions be employed for this purpose for all of the "major" milk proteins of raw skim milk except the immunoglobulins where, because of their heterogeneity and molecular genetics, physical parameters are less useful and their identification must be based upon antigenic determinants and their homology with their human counterparts. More work is needed and, with the accumulation of more information, additional changes in nomenclature can be expected for such proteins as the minor components of alphas- and kappa-caseins, alpha-lactalbumin, and the proteose-peptone fraction as well as further confirmation of the presence of immunoglobulins IgE and additional IgG subclasses. Additional components and genetic variants also can be expected.
The effect of pretreatment upon the composition and physicochemical and functional properties of whey, ultrafiltration (UF) retentate and freeze-dried and spray-dried whey protein concentrates (WPC) was investigated.Pretreatment was by cooling cheese whey to 0-5"C, adding calcium chloride, adjusting to pH 7.3, warming to 5o"C, and removing the insoluble precipitate that formed by centrifugation or decantation.UF permeation flux rate of pretreated whey was about double that for control whey. Pretreated whey was essentially turbidity free, contained 85% less milkfat, 37% more calcium and 40% less phosphorus than whey. Pretreated whey WPC proteins were slightly more soluble at pH 3, but less functional for emulsification than whey WPC proteins. Neither whey WPC proteins nor pretreated whey WPC proteins was functional for foaming at 6% protein concentration.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.