Milk Proteins in Prospect

McKenzie, H.A.

doi:10.1016/b978-0-12-485202-0.50019-1

Cited by 5 publications

(4 citation statements)

References 36 publications

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“…All equilibrium films were relatively thick common black films that were gray in color. The protein film was thicker than expected (29.9 nm) for a monolayer comparing with the molecular dimensions of the β-lactoglobulin dimers (3.6 × 3.6 × 6.9 nm) and the measured monolayer thickness obtained using neutron reflectivity or atomic force microscopy . However, it is in agreement with the thickness of foam films of β-lactoglobulin 11 at the low disjoining pressures employed by the dynamic thin film method and close to the thickness as indicated by the onset of the steric repulsion of disjoining pressure isotherms …”

Section: Resultssupporting

confidence: 78%

Disruption of Viscoelastic β-Lactoglobulin Surface Layers at the Air−Water Interface by Nonionic Polymeric Surfactants

et al. 2004

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Nonequilibrium interfacial layers formed by competitive adsorption of beta-lactoglobulin and the nonionic triblock copolymer PEO99-PPO65-PEO99 (F127) to the air-water interface were investigated in order to explain the influence of polymeric surfactants on protein film surface rheology and foam stability. Surface dilatational and shear rheological methods, surface tension measurements, dynamic thin-film measurements, diffusion measurements (from fluorescence recovery after photo bleaching), and determinations of foam stability were used as methods. The high surface viscoelasticity, both the shear and dilatational, of the protein films was significantly reduced by coadsorption of polymeric surfactant. The drainage rate of single thin films, in the presence of beta-lactoglobulin, increased with the amount of added F127, but equilibrium F127 films were found to be thicker than beta-lactoglobulin films, even at low concentration of the polymeric surfactant. It is concluded that the effect of the nonionic triblock copolymer on the interfacial rheology of beta-lactoglobulin layers is similar to that of low molecular weight surfactants. They differ however in that F127 increases the thickness of thin liquid films. In addition, the significant destabilizing effect of low molecular weight surfactants on protein foams is not found in the investigated system. This is explained as due to long-range steric forces starting to stabilize the foam films at low concentrations of F127.

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Section: Resultssupporting

confidence: 78%

Disruption of Viscoelastic β-Lactoglobulin Surface Layers at the Air−Water Interface by Nonionic Polymeric Surfactants

et al. 2004

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“…Table 4. Genetic variants of milk proteins of the genus Bos Data based on the work of Aschaffenburg (1968), McKenzie (1970McKenzie ( , 1971, Voglino (1972), Grosclaude et al (1976), Bell et al (1981) Before discussing these variants it is of interest to consider the origin of the Bali cattle in Australia from which we obtained our samples. It is known, as stated in Bell et al (1981), that the cattle were first brought from Indonesia to the military settlements of northern Australia over a century ago.…”

Section: Discussionmentioning

confidence: 99%

Bovine a-Lactalbumin C and aS1-, ß- and ?-Caseins of Bali (Banteng) Cattle, Bos (Bihos) Javanicus

Bell¹,

Hopper²,

Ha³

1981

Aust. Jnl. Of Bio. Sci.

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An electrophoretic examination is made of milk samples taken from eight Bali (banteng) cattle, Bos (Bibos) javanicus, at Beatrice Hills, Northern Territory, Australia. Starch-gel electrophoresis at pH 8· 5 (NaOH-H3B03 buffer) and filter-paper electrophoresis at pH 8· 6 (diethylbarbiturate buffer) indicate that all samples contain a new a-lactalbumin variant, designated a-lactalbumin C. The order of mobility for bovine variants is A > B > C. The C variant differs from the common B variant in having one more amide residue (substitution of Asn for Asp or GIn for Glu).Examination of milk samples by urea-starch-gel electrophoresis at alkaline pH indicates that there is a new asrcasein variant, designated as1-casein EBol;, present in some samples. No new K-casein variant is detected by this method (all samples typing as K-casein B). A new variant of jJ-casein, designated A4, is detected by urea-starch-gel electrophoresis at low pH.The variants of milk proteins observed in this paper and in Bell et al. (1981) are discussed in relation to those of other members of the Bovinae, especially the yak, Bos (Poephagus) grunniens.

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“…A number of techniques have been used to separate and analyze milk proteins: salt and organic solvent fractionation (McKenzie, 1971), starch gel electrophoresis (Aschaffenburg and Michalak, 1968), polyacrylamide gel electrophoresis (Andrews, 1981) isoelectric focussing (Trieu-Cuot and Gripon, 1981), as weil as combinations thereof. lon-exchange chromatography on DEAE cellulose and open-column gel permeation have been widely used, but the most significant advances have been achieved by applying high performance Iiquid chromatographic and fast protein liquid chromatographic techniques.…”

Section: Analysis Of Proteinsmentioning

confidence: 99%

Update on HPLC and FPLC analysis of nitrogen compounds in dairy products

Gonzalez-Llano

Polo

Ramos

1990

Lait

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Summary -HPLC and FPLC methods for the analysis of proteins, peptides, amino acids and amines in dairy products, as weil as their ability to resolve practical difficulties, are reviewed. The most pertinent Iiterature is summarized in tables giving the chromatographie conditions used in the analysis and the main objectives of each reference.HPLC 1 FPLC 1 dalry product 1 caseln 1 whey proteln 1 peptide 1 amino acld 1 nltrogen compound Résumé -L'analyse HPLC et FPLC des composés azotés dans les produits laitiers (synthèse). Cet article est une revue bibliographique concernant les méthodes HPLC et FPLC utilisées pour l'analyse des protéines, des peptides, des acides aminés et des amines dans les produits lai

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Milk Proteins in Prospect

Cited by 5 publications

References 36 publications

Disruption of Viscoelastic β-Lactoglobulin Surface Layers at the Air−Water Interface by Nonionic Polymeric Surfactants

Disruption of Viscoelastic β-Lactoglobulin Surface Layers at the Air−Water Interface by Nonionic Polymeric Surfactants

Bovine a-Lactalbumin C and aS1-, ß- and ?-Caseins of Bali (Banteng) Cattle, Bos (Bihos) Javanicus

Update on HPLC and FPLC analysis of nitrogen compounds in dairy products

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