scholarly journals Heat and/or high-pressure treatment of skim milk: changes to the casein micelle size, whey proteins and the acid gelation properties of the milk

2008 ◽  
Vol 61 (3) ◽  
pp. 245-252 ◽  
Author(s):  
SKELTE G. ANEMA
2004 ◽  
Vol 71 (1) ◽  
pp. 97-106 ◽  
Author(s):  
Thom Huppertz ◽  
Patrick F Fox ◽  
Alan L Kelly

Effects of high pressure (HP) on average casein micelle size and denaturation of α-lactalbumin (α-la) and β-lactoglobulin (β-lg) in raw skim bovine milk were studied over a range of conditions. Micelle size was not influenced by treatment at pressures <200 MPa, but treatment at 250 MPa increased micelle size by ∼25%, while treatment at [ges ]300 MPa irreversibly reduced it to ∼50% of that in untreated milk. The increase in micelle size after treatment at 250 MPa was greater with increasing treatment time and temperature and milk pH. Treatment times [ges ]2 min at 400 MPa resulted in similar levels of micelle disruption, but increasing milk pH to 7·0 partially stabilised micelles against HP-induced disruption. Denaturation of α-la did not occur [les ]400 MPa, whereas β-lg was denatured at pressures >100 MPa. Denaturation of α-la and β-lg increased with increasing pressure, treatment time and temperature and milk pH. The majority of denatured β-lg was apparently associated with casein micelles. These effects of HP on casein micelles and whey proteins in milk may have significant implications for properties of products made from HP-treated milk.


2006 ◽  
Vol 98 (3) ◽  
pp. 513-521 ◽  
Author(s):  
Vibeke Orlien ◽  
Jes C. Knudsen ◽  
Mireia Colon ◽  
Leif H. Skibsted

LWT ◽  
2015 ◽  
Vol 63 (1) ◽  
pp. 732-738 ◽  
Author(s):  
Sergio J. Ramos ◽  
Miriam Chiquirrín ◽  
Silvia García ◽  
Santiago Condón ◽  
María D. Pérez

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.


2006 ◽  
Vol 16 (4) ◽  
pp. 275-284 ◽  
Author(s):  
Hakim Bouaouina ◽  
Anne Desrumaux ◽  
Catherine Loisel ◽  
Jack Legrand

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