EDTA-induced dissociation of casein micelles and its effect on foaming properties of milk

1997 ◽  
Vol 64 (4) ◽  
pp. 495-504 ◽  
Author(s):  
BRENT R. WARD ◽  
SIMON J. GODDARD ◽  
MARY-ANN AUGUSTIN ◽  
IAN R. McKINNON

The effects of addition of EDTA on the dissociation of caseins and foaming properties of milks (100 g solids/l) reconstituted from skim milk powders given a low-heat (72°C for 30 s) or high-heat (85°C for 30 min) treatment during powder manufacture were determined. The EDTA-induced dissociation of caseins was independent of heat treatment but in high-heat milk was accompanied by release of denatured whey proteins. EDTA changed the proportions of individual caseins in the supernatant. EDTA addition improved both foam overrun and foam stability of low- and high-heat milks. The increase in serum protein on addition of EDTA contributed to the improvement in foaming properties of milks by increasing the availability of the proteins for formation of the air–water interface.

1993 ◽  
Vol 60 (2) ◽  
pp. 139-150 ◽  
Author(s):  
Theo J. M. Jeurnink ◽  
Kees G. De Kruif

SummarySkim milk was heated at 85 °C for different holding times. As a result of such heating, whey proteins, in particular β-lactoglobulin, denatured and associated with casein micelles. This led to an increase in size of the casein micelles but also to a different interaction between them. Both these changes could be described by using a quantitative model which was developed for the viscosity of so-called adhesive hard spheres. We applied the model successfully to skim milk and were able to describe on a quantitative basis the changes due to the heat treatment of milk. It was shown that after heating the casein micelles became larger and acquired a mutual attraction. The unfolding of the whey proteins and their subsequent association with the casein micelles appeared to be responsible for these changes. How this reaction influences the fouling of heat exchangers is discussed.


1998 ◽  
Vol 65 (4) ◽  
pp. 555-567 ◽  
Author(s):  
JOHN A. LUCEY ◽  
MICHELLE TAMEHANA ◽  
HARJINDER SINGH ◽  
PETER A. MUNRO

The effect of interactions of denatured whey proteins with casein micelles on the rheological properties of acid milk gels was investigated. Gels were made by acidification of skim milk with glucono-δ-lactone at 30°C using reconstituted skim milk powders (SMP; both low- and ultra-low-heat) and fresh skim milk (FSM). The final pH of the gels was ∼4·6. Milks containing associated or ‘bound’ denatured whey proteins (BDWP) with casein micelles were made by resuspending the ultracentrifugal pellet of heated milk in ultrafiltration permeate. Milks containing ‘soluble’ denatured whey protein (SDWP) aggregates were formed by heat treatment of an ultracentrifugal supernatant which was then resuspended with the pellet. Acid gels made from unheated milks had low storage moduli, G′, of <20 Pa. Heating milks at 80°C for 30 min resulted in acid gels with G′ in the range 390–430 Pa. The loss tangent (tan δ) of gels made from heated milk increased after gelation to attain a maximum at pH ∼5·1, but no maximum was observed in gels made from unheated milk. Acid gels made from milks containing BDWP that were made from low-heat SMP, ultra-low-heat SMP and FSM had G′ of about 250, 270 and 310 Pa respectively. Acid gels made from milks containing SDWP that were made from ultra-low-heat SMP or FSM had G′ values in the range 17–30 Pa, but gels made from low-heat SMP had G′ of ∼140 Pa. It was concluded that BDWP were important for the increased G′ of acid gels made from heated milk. Addition of N-ethylmaleimide (NEM) to low-heat reconstituted milk, to block the —SH groups, resulted in a reduction of the G′ of gels formed from heated milk but did not reduce G′ to the value of unheated milk. Addition of 20 mm-NEM to FSM, prior to heat treatment, resulted in gels with a lower G′ value than gels made from reconstituted low-heat SMP. It was suggested that small amounts of denatured whey proteins associated with casein micelles during low-heat SMP manufacture were probably responsible for the higher G′ of gels made from milk containing SDWP and from milk heated in the presence of 20 mm-NEM, compared with gels made from FSM.


2003 ◽  
Vol 70 (1) ◽  
pp. 73-83 ◽  
Author(s):  
Skelte G Anema ◽  
Yuming Li

When skim milk at pH 6·55 was heated (75 to 100 °C for up to 60 min), the casein micelle size, as monitored by photon correlation spectroscopy, was found to increase during the initial stages of heating and tended to plateau on prolonged heating. At any particular temperature, the casein micelle size increased with longer holding times, and, at any particular holding time, the casein micelle size increased with increasing temperature. The maximum increase in casein micelle size was about 30–35 nm. The changes in casein micelle size were poorly correlated with the level of whey protein denaturation. However, the changes in casein micelle size were highly correlated with the levels of denatured whey proteins that were associated with the casein micelles. The rate of association of the denatured whey proteins with the casein micelles was considerably slower than the rate of denaturation of the whey proteins. Removal of the whey proteins from the skim milk resulted in only small changes in casein micelle size during heating. Re-addition of β-lactoglobulin to the whey-protein-depleted milk caused the casein micelle size to increase markedly on heat treatment. The changes in casein micelle size induced by the heat treatment of skim milk may be a consequence of the whey proteins associating with the casein micelles. However, these associated whey proteins would need to occlude a large amount of serum to account for the particle size changes. Separate experiments showed that the viscosity changes of heated milk and the estimated volume fraction changes were consistent with the particle size changes observed. Further studies are needed to determine whether the changes in size are due to the specific association of whey proteins with the micelles or whether a low level of aggregation of the casein micelles accompanies this association behaviour. Preliminary studies indicated lower levels of denatured whey proteins associated with the casein micelles and smaller changes in casein micelle size occurred as the pH of the milk was increased from pH 6·5 to pH 6·7.


1997 ◽  
Vol 64 (4) ◽  
pp. 591-600 ◽  
Author(s):  
JOHN A. LUCEY ◽  
CHENG TET TEO ◽  
PETER A. MUNRO ◽  
HARJINDER SINGH

The effect of a range of milk heat treatments on the rheological properties, at small and large deformations, of acid skim milk gels was investigated. Gels were made from reconstituted skim milk heated at 75, 80, 85 and 90°C for 15 or 30 min by acidification with glucono-δ-lactone at 30°C. Gels were also made from skim milk powder (SMP) samples that had been given a range of preheat treatments during powder manufacture. Heating milks at temperatures [ges ]80°C for 15 min increased the storage moduli (G′) compared with unheated milk and produced gels with G′ in the range 300–450 Pa. Acid gels made from high-heat or medium-heat SMP had higher G′ than gels made from low-heat or ultra-low-heat SMP. Cooling gels to low temperatures resulted in an increase in G′. The yield stress of gels slightly decreased with mild heat treatments of milk, and then increased again to a maximum, finally decreasing slightly with very high heat treatments of milk. The strain at yielding decreased markedly with increasing heat treatment of milk, making these gels brittle and easier to fracture. We propose that denatured whey proteins aggregated with casein particles during the acidification of heated milk and were responsible for most of the effects observed in this study.


2007 ◽  
Vol 5 (18) ◽  
pp. 47-54 ◽  
Author(s):  
A.P.J Middelberg ◽  
L He ◽  
A.F Dexter ◽  
H.-H Shen ◽  
S.A Holt ◽  
...  

We report the structure and Young's modulus of switchable films formed by peptide self-assembly at the air–water interface. Peptide surfactant AM1 forms an interfacial film that can be switched, reversibly, from a high- to low-elasticity state, with rapid loss of emulsion and foam stability. Using neutron reflectometry, we find that the AM1 film comprises a thin (approx. 15 Å) layer of ordered peptide in both states, confirming that it is possible to drastically alter the mechanical properties of an interfacial ensemble without significantly altering its concentration or macromolecular organization. We also report the first experimentally determined Young's modulus of a peptide film self-assembled at the air–water interface ( E =80 MPa for AM1, switching to E <20 MPa). These findings suggest a fundamental link between E and the macroscopic stability of peptide-containing foam. Finally, we report studies of a designed peptide surfactant, Lac21E, which we find forms a stronger switchable film than AM1 ( E =335 MPa switching to E <4 MPa). In contrast to AM1, Lac21E switching is caused by peptide dissociation from the interface (i.e. by self-disassembly). This research confirms that small changes in molecular design can lead to similar macroscopic behaviour via surprisingly different mechanisms.


Soft Matter ◽  
2020 ◽  
Vol 16 (15) ◽  
pp. 3695-3704 ◽  
Author(s):  
Xiuying Qiao ◽  
Reinhard Miller ◽  
Emanuel Schneck ◽  
Kang Sun

Silk fibroin (SF) adsorbs at the air/water interface, reduces the surface tension, and forms interfacial layers suppressing bubble coalescence and stabilizing foam.


2001 ◽  
Vol 68 (3) ◽  
pp. 471-481 ◽  
Author(s):  
CATHERINE SCHORSCH ◽  
DEBORAH K. WILKINS ◽  
MALCOLM G. JONES ◽  
IAN T. NORTON

The aim of the present work was to investigate the role of whey protein denaturation on the acid induced gelation of casein. This was studied by determining the effect of whey protein denaturation both in the presence and absence of casein micelles. The study showed that milk gelation kinetics and gel properties are greatly influenced by the heat treatment sequence. When the whey proteins are denatured separately and subsequently added to casein micelles, acid-induced gelation occurs more rapidly and leads to gels with a more particulated microstructure than gels made from co-heated systems. The gels resulting from heat-treatment of a mixture of pre-denatured whey protein with casein micelles are heterogeneous in nature due to particulates formed from casein micelles which are complexed with denatured whey proteins and also from separate whey protein aggregates. Whey proteins thus offer an opportunity not only to control casein gelation but also to control the level of syneresis, which can occur.


2010 ◽  
Vol 345 (1) ◽  
pp. 54-63 ◽  
Author(s):  
Najet Mahmoudi ◽  
Cédric Gaillard ◽  
François Boué ◽  
Monique A.V. Axelos ◽  
Alain Riaublanc

2000 ◽  
Vol 67 (1) ◽  
pp. 31-42 ◽  
Author(s):  
ERIC C. NEEDS ◽  
ROBERT A. STENNING ◽  
ALISON L. GILL ◽  
VICTORIA FERRAGUT ◽  
GILLIAN T. RICH

High isostatic pressures up to 600 MPa were applied to samples of skim milk before addition of rennet and preparation of cheese curds. Electron microscopy revealed the structure of rennet gels produced from pressure-treated milks. These contained dense networks of fine strands, which were continuous over much bigger distances than in gels produced from untreated milk, where the strands were coarser with large interstitial spaces. Alterations in gel network structure gave rise to differences in rheology with much higher values for the storage moduli in the pressure-treated milk gels. The rate of gel formation and the water retention within the gel matrix were also affected by the processing of the milk. Casein micelles were disrupted by pressure and disruption appeared to be complete at treatments of 400 MPa and above. Whey proteins, particularly β-lactoglobulin, were progressively denatured as increasing pressure was applied, and the denatured β-lactoglobulin was incorporated into the rennet gels. Pressure-treated micelles were coagulated rapidly by rennet, but the presence of denatured β-lactoglobulin interfered with the secondary aggregation phase and reduced the overall rate of coagulation. Syneresis from the curds was significantly reduced following treatment of the milk at 600 MPa, probably owing to the effects of a finer gel network and increased inclusion of whey protein. Levels of syneresis were more similar to control samples when the milk was treated at 400 MPa or less.


2010 ◽  
Vol 81 (1) ◽  
pp. 50-57 ◽  
Author(s):  
Adrián A. Perez ◽  
Cecilio Carrera Sánchez ◽  
Juan M. Rodríguez Patino ◽  
Amelia C. Rubiolo ◽  
Liliana G. Santiago

Sign in / Sign up

Export Citation Format

Share Document