scholarly journals Optimisation of a whey protein fractionation process based on the selective precipitation of α-lactalbumin

1997 ◽  
Vol 77 (3) ◽  
pp. 411-423 ◽  
Author(s):  
C. Bramaud ◽  
P. Aimar ◽  
G. Daufin
2011 ◽  
Vol 78 (2) ◽  
pp. 196-202 ◽  
Author(s):  
Ayoa Fernández ◽  
Violeta Menéndez ◽  
Francisco A Riera ◽  
Ricardo Álvarez

This work studied the behaviour of caseinomacropeptide (CMP) in a whey protein fractionation process based on the selective precipitation of α-lactalbumin (α-la) in an acid medium. Three different acids (hydrochloric, citric and lactic) and different operating conditions (protein concentration, temperature and pH) were considered to perform the precipitation step. Under the optimised precipitation conditions obtained for α-la (pH 4, 55°C, initial α-la concentration around 12 g/l) CMP presents quite similar behaviour to that observed for β-lactoglobulin (β-lg), namely remaining in the supernatant fraction. However, at a lower pH value (3·5) the amount of precipitated CMP increases up to 72% when citric acid is added. This behaviour could be due to the fact that CMP is close to its isoelectric point, which allows a supernatant fraction enriched in β-lg that is almost free from the rest of proteins in sweet whey.


Author(s):  
Laetitia M. Bonnaillie ◽  
Peggy M. Tomasula

1974 ◽  
Vol 57 (7) ◽  
pp. 793-796 ◽  
Author(s):  
R.L. Richter ◽  
C.V. Morr ◽  
G.A. Reineccius

2011 ◽  
Vol 33 (8) ◽  
pp. 1501-1511 ◽  
Author(s):  
Mayyada M. H. El-Sayed ◽  
Howard A. Chase

Foods ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1090
Author(s):  
Simon Schiffer ◽  
Bello Teslim Adekunle ◽  
Andreas Matyssek ◽  
Martin Hartinger ◽  
Ulrich Kulozik

During skim milk microfiltration (nominal pore size of 0.1 µm) at 10 °C, the whey protein purity in the permeate is reduced by an enhanced serum casein permeation, primarily of β-casein. To decrease casein permeation, the possibility of a pre-heating step under pasteurization conditions before the filtration step was investigated, so as to shift the equilibrium from soluble serum casein monomers to impermeable micellar casein. Immediately after the pre-heating step, low temperature microfiltration at 10 °C was conducted before the casein monomers could diffuse into the serum. The hypothesis was that the dissociation of β-casein into the serum as a result of a decreasing temperature takes more time than the duration of the microfiltration process. It was found that pre-heating reduced the β-casein permeation during microfiltration without significantly affecting the flux and whey protein permeation, compared with a microfiltration at 10 °C without the pre-heating step. Furthermore, the addition of calcium (5 and 10 mM) not only reduced the casein permeation and thus increased the permeate purity, defined as a high whey protein-to-casein (g L−1/g L−1) ratio, but also decreased the filtration performance, possibly due to the structural alteration of the deposited casein micelle layer, rendering the deposit more compact and more retentive. Therefore, the possible combination of the addition of calcium and pre-heating prior to microfiltration was also investigated in order to evidence the potential increase of whey protein (WP) purity in the permeate in the case of Ca2+ addition prior to microfiltration. This study shows that pre-heating very close to low temperature microfiltration results in an increased purity of the whey protein fraction obtained in the permeate.


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