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Pilot-scale microfiltration (MF), microfiltration-diafiltration (MDF), ultrafiltration (UF), ultrafiltration-diafiltration (UDF), and nanofilration (NF) membrane fractionation processes were designed and evaluated for removing 90% to 95% of the lactose and sodium from skim milk. The study was designed to evaluate several membrane fractionation schemes as a function of: (1) membrane types with and without diafiltration; (2) fractionation process temperatures ranging from 17 to 45 degrees C; (3) sources of commercial drinking water used as diafiltrant; and (4) final mass concentration ratios (MCR) ranging from about 2 to 5. MF and MDF membranes provided highest flux values, but were unsatisfactory because they failed to retain all of the whey proteins. UDF fractionation processes removed more than 90% to 95% of the lactose and sodium from skim milk. NF permeate prepared from UDF cumulative permeate contained sodium and other mineral concentrations that would make them unsuitable for use as a diafiltrant for UDF applications. A method was devised for preparing simulated milk permeate (SMP) formulated with calcium, magnesium, and potassium hydroxides, and phosphoric and citric acids for use as UDF diafiltrant or for preparing lactose and sodium reduced skim milk (L-RSM). MF retentates with MCR values of 4.7 to 5.0 exhibited extremely poor frozen storage stabilities of less than 1 wk at -20 degrees C, whereas MCR 1.77 to 2.95 MDF and UDF retentates and skim milk control exhibited frozen storage stabilities of more than 16 wk. L-RSM exhibited a whiter appearance and a lower viscosity than skim milk, lacked natural milk flavor, and exhibited a metallic off-flavor.

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Results of this study confirm that high temperature (118 degrees C/15 min) and high pressure (400 MPa/5 min) processing of skim milk, skim milk ultrafiltration and ultracentrifugation fractions, and model milk salt solutions cause dramatic shifts in their colloidal and soluble Ca phosphate equilibrium that affect their pH, dissolved Ca content, turbidity, and casein micelle microstructure. The relations between high temperature and high pressure processing-induced changes in the colloidal and soluble Ca phosphate equilibrium were evaluated in raw, pasteurized, and high temperature treated skim milk, ultrafiltration retentate and permeate of pasteurized skim milk, clear ultracentrifugation infranatant of pasteurized skim milk, and synthetic milk ultrafiltrates with and without lactose or Ca. The magnitude of the pH and dissolved Ca shifts caused by high temperature and high pressure processing was a function of casein micelle concentration. Ultrafiltration permeate exhibited the most drastic shits in pH and dissolved Ca contents due to high temperature and high pressure processing. Although high temperature processing reduced the pH of ultrafiltration permeate from 6.59 to 6.03 and the dissolved Ca from 100% to 58%, high pressure processing reversed both of these changes. These changes in high temperature and high pressure processed milk, milk fractions, and model milk salt solutions were related to microstructural changes in the casein micelles as revealed by electron microscopy.

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Substantial progress has been made in understanding the basic chemical and structural properties of the principal whey proteins, that is, beta-lactoglobulin (beta-Lg), alpha-lactalbumin (alpha-La), bovine serum albumin (BSA), and immunoglobulin (Ig). This knowledge has been acquired in terms of: (1) procedures for isolation, purification, and characterization of the individual whey proteins in buffer solutions; and (2) whey fractionation technologies for manufacturing whey protein concentrates (WPC) with improved chemical and functional properties in food systems. This article is a critical review of selected publications related to (1) whey fractionation technology for manufacturing WPC and WPI; (2) fundamental properties of whey proteins; and (3) factors that affect protein functionality, that is, composition, protein structure, and processing.

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The modern food-processing industry is placing more and more emphasis upon the utilization of protein ingredients to provide specific functional properties to a wide range of formulated foods. Isolated milk protein products represent an important and valuable source of protein ingredients due to their recognized superior nutritional, organoleptic and functional properties. This paper provides up-to-date information on the quantities, production processes, composition, general properties, and specific functional properties of the major milk protein products, e.g. caseinates, co-precipitates, lactalbumin, whey protein concentrates and milk blends. The subject of chemical and enzymic modification to improve certain functional properties of milk proteins is considered briefly.

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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.

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This paper analyzes the current knowledge of mild protein chemistry to explain the reactions and their control for the major processes utilized by the modern milk processing industry. The compositon and chemical properties of casein micelles and whey proteins are summarized. The effect of processing upon denaturation, aggregration, and destabilization of milk proteins is updated. The role of milk proteins in the gelation of sterile milk concentrates, destabilization of frozen milk, rennet-clotting of milk, and stabilization of the fat emulsion in milk is also described.

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