C. Bramaud et al., OPTIMIZATION OF A WHEY-PROTEIN FRACTIONATION PROCESS-BASED ON THE SELECTIVE PRECIPITATION OF ALPHA-LACTALBUMIN, Le Lait, 77(3), 1997, pp. 411-423
Whey protein fractionation based on the selective isoelectric precipit
ation of alpha-lactalbumin has been optimised by an overall approach.
Precipitation phenomena and rheological characteristics of the fluid a
fter heat treatment have both been considered. Control of calcium conc
entration, a new operating parameter, has optimised the precipitation
step. A reduction of this concentration leads to an increase in the al
pha-lactalbumin fraction precipitated at a moderate protein concentrat
ion. The use of citric acid, a calcium complexation agent, is proposed
. It permits simultaneous adjustment of the pH and a reduction in the
free calcium concentration. Co-precipitation of immunoglobulins and bo
vine serum albumin has been studied. However, there are no conditions
under which alpha-lactalbumin is the only protein that precipitates. T
o separate precipitated and soluble fractions, centrifugation is the m
ethod proposed, as it is more efficient than microfiltration. After so
lubilisation, the two forms of alpha-lactalbumin may be recovered: the
apo-alpha-lactalbumin with a calcium-free solvent, and the native for
m with a calcium solvent. When a solution of calcium chloride is used,
solubilisation is a fractionation step (increase of 23% in alpha-LA p
urity), as the immunoglobulins remain insoluble.