Determination of tensile strength of gels prepared from fractionated whey proteins

1986 ◽  
Vol 53 (2) ◽  
pp. 285-292 ◽  
Author(s):  
Keith R. Langley ◽  
David Millard ◽  
E. William Evans

SUMMARYA novel method for measuring tensile strength of heat-setting gels is described and is applied to whey protein gels. Contributions made by β-lactoglobulin and α-lactalbumin individually to the tensile strength of the gel are calculated. The tensile strength can be found from power law equations related to concentration of α-lactalbumin and β-lactoglobulin in whey protein mixtures.

1989 ◽  
Vol 56 (2) ◽  
pp. 211-222 ◽  
Author(s):  
Pierre Lambelet ◽  
Rafael Berrocal ◽  
Francine Ducret

SummaryA method using low resolution NMR spectroscopy is described for investigating whey protein thermal denaturation. The method is based on measuring at 20 °C changes in water proton transverse (T2) relaxation parameter following the denaturing treatment. This parameter is shown to be sensitive to protein denaturation and not to other phenomena such as gelation. Examples are given for the qualitative study of protein thermal denaturation in whey protein concentratc, β-lactoglobulin, α-lactalbumin, bovine serum albumin and immunoglobulins aqueous solutions and for the quantitative determination of thermal denaturation in whey protein concentrate solutions.


1985 ◽  
Vol 52 (4) ◽  
pp. 529-538 ◽  
Author(s):  
Harjinder Singh ◽  
Partick F. Fox

SUMMARYPreheating milk at 140 °C for 1 min at pH 6·6, 6·8, 7·0 or 7·2 shifted the heat coagulation time (HCT)/pH profile to acidic values without significantly affecting the maximum stability. Whey proteins (both β-lactoglobulin and α-lactalbumin) co-sedimented with the casein micelles after heating milk at pH < 6·9 and the whey protein-coated micelles, dispersed in milk ultrafiltrate, showed characteristic maxima–minima in their HCT/pH profile. Heating milk at higher pH values (> 6·9) resulted in the dissociation of whey proteins and κ-casein-rich protein from the micelles and the residual micelles were unstable, without a maximum–minimum in the HCT/pH profile. Preformed whey protein–casein micelle complexes formed by preheating (140 °C for 1 min) milk at pH 6·7 dissociated from the micelles on reheating (140 °C for 1 min) at pH > 6·9. The dissociation of micellar-κ-casein, perhaps complexed with whey proteins, may reduce the micellar zeta potential at pH ≃ 6·9 sufficiently to cause a minimum in the HCT/pH profile of milk.


1993 ◽  
Vol 60 (1) ◽  
pp. 55-63 ◽  
Author(s):  
M. Dolores Pérez ◽  
Pilar Puyol ◽  
José Manuel Ena ◽  
Miguel Calvo

SummaryThe interaction of sheep, horse, pig, human and guinea-pig whey proteins with fatty acids has been studied. Using gel filtration and autoradiography, it was found that sheep β-lactoglobulin and serum albumin from all species had the ability to bind fatty acids in vitro. Sheep β-lactoglobulin, isolated from milk, had ˜ 0·5 mol fatty acids bound per mol monomer protein, and albumin from sheep, horse and pig contained ˜ 4·5, 2·9 and 4·7 mol fatty acids/mol protein respectively. However, β-lactoglobulin from horse and pig milk had neither fatty acids physiologically bound nor the ability to bind them in vitro. Albumin was the only whey protein detected with bound fatty acids in these species as well as in human and guinea pig. This suggests that the ability of ruminant β-lactoglobulin to bind fatty acids was not shared by the same protein of non-ruminants.


2005 ◽  
Vol 85 (1) ◽  
pp. 93-99 ◽  
Author(s):  
A. Summer ◽  
A. Tirelli ◽  
P. Formaggioni ◽  
M. Malacarne ◽  
P. Mariani

The aim of this research was to describe the changes of the nitrogen fractions in milk of Haflinger nursing mares and in particular to determine the whey protein content and distribution, and their evolution throughout the first 6 mo of lactation. Samples were collected by hand-milking on days 4, 20, 40, 60, 80, 120, 150 and 180 post-partum. Nitrogen fractions were determined by Kjeldahl on 80 samples from 10 mares, while HPLC separation of whey proteins was conducted on 40 samples from 5 mares. The total N, casein N, and true whey protein N contents showed a statistically significant decrease from day 4 to day 40, and then remained unvaried. In general, the nitrogen distribution of mare’s milk significantly changed between day 4 and day 20 and then remained almost unchanged until day 180 (except for the day 150 value, which showed a statistically significant increase for CN × 100/TN). β-Lactoglobulin and serum albumin contents showed a marked reduction, of 27 and 45.5%, respectively, between day 4 and day 20, and then remained unchanged; α-lactalbumin and immunoglobulins contents had a reduction of 24.7 and 38.3%, respectively, between day 4 and day 20, and another decrease between day 20 and day 40, of 20 and 32.8%, respectively. All whey proteins, expressed as a percentage on the total sum of the four whey proteins considered, did not vary significantly during lactation. However, the sum on the two whey proteins of mammary gland origin (β-Lg + α-La) increased between day 4 and day 20 by 6.3%, and between day 20 and day 40 by 3.8%; the sum of the whey proteins of blood origin (SA + Ig) showed an opposite trend, with a decrease by 14.5% between day 4 and day 20 and by 11% between day 20 and day 40. Key words: Mare’s milk, lactation stage, whey protein distribution, reversed-phase HPLC


Author(s):  
D. L. May ◽  
A. P. Gordon ◽  
D. S. Segletes

Accurate determination of constitutive modeling constants used in high value components, especially in electric power generation equipment, is vital for related design activities. Parts under creep are replaced after extensive deformation is reached, so models, such as the Norton-Bailey power law, support service life prediction and repair/replacement decisions. For high fidelity calculations, experimentally acquired creep data must be accurately regressed over a variety of temperature, stress, and time combinations. If these constants are not precise, then engineers could be potentially replacing components with lives that have been fractionally exhausted, or conversely, allowing components to operate that have already been exhausted. By manipulating the Norton-Bailey law and utilizing bivariate power-law statistical regression, a novel method is introduced to precisely calculate creep constants over a variety of sets of data. The limits of the approach are explored numerically and analytically.


2005 ◽  
Vol 72 (3) ◽  
pp. 369-378 ◽  
Author(s):  
David J Oldfield ◽  
Harjinder Singh ◽  
Mike W Taylor

Microfiltration and ultrafiltration were used to manufacture skim milks with an increased or reduced concentration of whey proteins, while keeping the casein and milk salts concentrations constant. The skim milks were heated on a pilot-scale UHT plant at 80, 90 and 120 °C. The heat-induced denaturation and aggregation of β-lactoglobulin (β-lg), α-lactalbumin (α-la) and bovine serum albumin (BSA) were quantified by polyacrylamide gel electrophoresis. Apparent rate constants and reaction orders were calculated for β-lg, α-la and BSA denaturation. Rates of β-lg, α-la and BSA denaturation increased with increasing whey protein concentration. The rate of α-la and BSA denaturation was affected to a greater extent than β-lg by the change in whey protein concentration. After heating at 120 °C for 160 s, the concentration of β-lg and α-la associated with the casein micelles increased as the initial concentration of whey proteins increased.


1964 ◽  
Vol 31 (1) ◽  
pp. 41-51 ◽  
Author(s):  
R. L. J. Lyster

SummaryA new method is described for the determination of the free and masked sulphydryl (-SH) groups in heated milk and milk products. The procedure is based on the use of the specific -SH reagent p-chloromercuribenzoate, and utilizes another specific -SH reagent, 5,5' -dithiobis(2-nitrobenzoate), as an indicator producing yellow colours which are matched with the aid of standard glasses in the Lovibond Comparator.The method was applied to heated skim-milks and a series of commercially prepared milk powders. Measurements were made in particular of the -SH content of UHT-treated milk. The changes in the -SH content of such milks on storage were studied; these changes could not be explained by a reversal of the denaturation of the whey proteins, although evidence was obtained that small amounts of heatdenatured whey protein can revert to the native state.


1980 ◽  
Vol 47 (3) ◽  
pp. 337-342 ◽  
Author(s):  
Thomas G. Parker ◽  
David S. Horne

SUMMARYThe turbidity increase on storage of milk dialysate was shown to be due to Ca phosphate precipitation. The rate of precipitation at 40 °C could be decreased by shortening the duration of dialysis or by the addition of small amounts of EDTA. The dialysate was stabilized against Ca phosphate precipitation by the addition of the whey protein fraction of milk. Individual whey proteins varied in their stabilizing ability: α-lactalbumin was found to be more effective than β-lactoglobulin which gave approximately the same effect as an immunoglobulin fraction. BSA and lysozyme had a destabilizing effect and ovalbumin possessed a slight stabilizing ability.


2013 ◽  
Vol 31 (No. 3) ◽  
pp. 211-216 ◽  
Author(s):  
M. Tomczyńska-Mleko

The microstructure and stability of aerated whey protein gels were determined. Foamed whey protein gels were obtained using a novel method applying a simultaneous gelation and aeration process. Whey protein gels were produced at different protein concentrations and pH by calcium ion induction at ambient temperature. Two concentrations of calcium ions were used: 20 and 30mM to produce foamed gels with different microstructure. Foamed gels obtained at 30mM Ca<sup>2+</sup> were composed of thick strands and irregular, large air bubbles. For these gels, larger synaeresis and bubble size reduction were observed. Fine-stranded, small bubble size aerated gels obtained at 20mM Ca<sup>2+</sup> were very stable during storage. Decreased protein concentration and increased pH of the gels resulted in an increased bubble size. &nbsp;


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