"Ferripolyphosphate" as a whey protein precipitant

Jones, Susan B.; Kalan, Edwin B.; Jones, Thomas C.; Hazel, J. Frederick

doi:10.1021/jf60180a021

Cited by 38 publications

(14 citation statements)

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“…Iron complexes previously have been produced in an effort to find iron supplements of high bioavailability yet low reactivity in food systems. These have included complexing ferric iron with phenolic compounds (Parliment, 1977;Scarpellino, 1977), a ferripolyphosphate-whey protein complex (Jones et al, 1972;Amantea et al, 1974), and ironphytate complexes (Morris and Ellis, 1976). The ferripolyphosphate-whey protein powder has been used as an iron supplement in milk, where the iron was 84-107% assimilable (Jones et al, 1975), and in flour and flour-containing products (Nimmo and Fellers, 1975).…”

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confidence: 99%

Iron Availability From Wheat Gluten, Soy Isolate, and Casein Complexes

Nelson¹,

Potter²

1980

Journal of Food Science

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Release of iron bound to animal and vegetable protein sources was investigated. Ferrous and ferric iron complexes with wheat gluten, soy protein isolate, and casein were prepared under conditions shown to bind large quantities of iron to the insoluble residue. These mixtures were lyopbihzed and ground to a fiie powder. Treatment of the 1yophIlized protein-iron-mixtures with O.lN HCl released 30-68% of the bound iron. Digestion in an HCl-pepsin or an HCl-pepsin-pancreatin system released 64-94% and 85-97% of the bound iron, respectively, indicating that protein-bound iron should be readily freed for absorption within the gastrointestinal tract. Using the hemoglobin repletion technique, protein-bound ferrous iron was statistically as biologically avaiIable as the standard, ferrous sulfate. Estimates of the relative biological values for the protein-ferric mixtures were somewhat lower than reported in the literature for ferric pyrophosphate, the free salt used in binding.

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confidence: 99%

Iron Availability From Wheat Gluten, Soy Isolate, and Casein Complexes

Nelson¹,

Potter²

1980

Journal of Food Science

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“…Gel filtration has been adapted to the commercial preparation of some whey products, either as a column or centrifugal (Morr, Nielsen & Coulter, 1967) process, while one of the oldest methods simply relies on the heat precipitation of protein. A number of isolation techniques have made use of precipitation by complex formation with long chain polyphosphates, such as hexametaphosphate (Richert, 1975), or ferripolyphosphate (Jones et al 1972), but one of the most interesting developments involves complexing whey protein with carboxymethylcellulose (CMC) (Zadow & Hill, 1975;Palmer, 1977). The CMC can be subsequently removed at alkaline pH, yielding a product which is capable of forming stable foams and gels.…”

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confidence: 99%

Thermal denaturation of α-lactalbumin and β-lactoglobulin in cheese whey: effect of total solids concentration and pH

Hillier¹,

Lyster²,

Cheeseman³

1979

Journal of Dairy Research

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Measurements of residual native protein remaining after heat treatment of cheese whey have been made using quantitative polyacrylamide gel electrophoresis. The results have been expressed in terms of kinetic constants. The effect of concentration was investigated up to 3 times the normal total solids content, dialysis treatments were used to study the effect of non-protein constituents, and the effect of pH was studied at pH 4, 6 and 9. The results indicated that increased total solids (TS) concentration slowed the denaturation of /9-lactoglobulin A and B (/?-lg A, yff-lg B) but hastened the denaturation of a-lactalbumin (a-la). However, increased lactose concentration slowed the denaturation of both a-la and /ff-lg, perhaps by preventing formation of heat-induced complexes. Increased Ca concentration, up to 0-4 mg/ml, tended to slow the denaturation of both proteins, but further increase in Ca up to 0-9 mg/ml produced little effect. The rate of denaturation of both a-la and /#-lg was slower at pH 4 than at pH 6 or 9, and was probably slowest at the isoelectric point. However, not all the changes associated with pH could be explained in terms of net molecular electrostatic charge. The genetic variants of '/?-lg showed different heat stabilities -below 90 °C /?-lgA was more stable than /MgB, but above 90 °C the situation was reversed at all TS concentrations, and pH 6. However, at pH 4 and 9, yff-lg A was less stable than /?-lgB over the entire temperature range at normal concentration.

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“…This finding was subsequently extended to bovine muscle and to a number of other modifiers including EDTA by Robson (Go11 and Robson, 1967;Robson et al, 1967) and to chicken muscle by measuring Mg2+-ATPase by Jones (1972). I t is, however, to be mentioned that changes in Mg2+-ATPase of myosin B or myofibrils at low ionic strength during storage may not be only a measure of actin-myosin interaction, but rather a manifestation of the proteolytic degradation occurring in the regulatory protein, troponin complex.…”

Section: Discussionmentioning

confidence: 83%

Stability of myofibrillar EDTA-ATPase in rabbit psoas fiber bundles

Yasui¹,

Sumita²,

Tsunogae³

1975

J. Agric. Food Chem.

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The rate and extent of inactivation of myofibrillar EDTA-ATPase in rabbit psoas fiber bundles at various temperatures between 3 and 42' and a t pH values between 5.5 and 7.0 have been studied by measuring the EDTA-ATPase activity. The purification of psoas myofibrils with Triton X-100 permitted the direct measurement of changes in the myofibrillar ATPase activity of psoas fiber bundles stored under various conditions. The myofibrillar ATPase, when the fiber bundles are stored in the medium a t 3' and pH 5.5, are quite stable. During storage a t 3O for 72 hr, it has been found that myofibrillar ATPase activity remained almost constant between pH 5.5 and 7.0. However, at higher temperatures, the rate of thermal inactivation is increased in the more acidic systems. From the results it has been concluded that the effect, of pH on the loss of myofibrillar ATPase is negligible if the fiber bundles are stored near 0' and that the most important factor influencing the denaturation is the temperature at which the fiber bundles are stored.A naturally occurring phenomenon of some interest is the so-called PSE (pale, soft, and exudative), or watery condition in some types of pig muscle. The condition is characterized by a very rapid pH fall postmortem, and by soft, pale, and watery musculature in the post-rigor state (Briskey and Wismer-Pedersen, 1961;Bendall and Lawrie, 1964;Briskey, 1964). Whale, beef, and rabbit muscles, subjected to high temperature rigor, also develop wateriness, so the condition is of general occurrence under these conditions and is not peculiar to pigs (Bendall and WismerPedersen, 1962;Bendall and Lawrie, 1964). Penny (1967) and Yasui e t al. (1973) were able to show that myosin B (natural actomyosin) and myosin prepared from rabbit muscle were considerably denatured under these conditions. These authors demonstrated that both types of protein were sensitive to temperature and pH in the range to be expected in a cooling carcass, i.e., 36-38' and a pH of 6.0 or below within 1 hr of death in those samples exhibiting the highest rate of glycolysis. We can therefore attribute the PSE phenomenon principally to protein denaturation at high temperature and low pH.In order to investigate what actually occurs in intact muscle during rigor, it is desirable to use a highly organized muscle model whose structural features are similar to that of intact muscle. Yasui et al. (1973) studied the denaturation of myosin in glycerol-treated fiber bundles, which were fixed t o application rods a t rest length, using extractability and Ca*+-ATPase activity as criteria. Their results indicated that the protein in the fiber bundles was more stable than the isolated protein molecules.T o confirm and extend the conclusion derived from their study, the preferred approach was to investigate directly the myofibrillar ATPase under the conditions of temperature and pH encountered in practice. This has not been done so far for the following two reasons. (1) When the washed myofibrils are exposed to severe conditions, e.g., high...

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"Ferripolyphosphate" as a whey protein precipitant

Cited by 38 publications

References 4 publications

Iron Availability From Wheat Gluten, Soy Isolate, and Casein Complexes

Iron Availability From Wheat Gluten, Soy Isolate, and Casein Complexes

Thermal denaturation of α-lactalbumin and β-lactoglobulin in cheese whey: effect of total solids concentration and pH

Stability of myofibrillar EDTA-ATPase in rabbit psoas fiber bundles

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