Preparation of β‐Lactoglobulin and p‐Lactoglobulin‐Free Proteins from Whey Retentate by NaCI Salting Out at Low pH
P. MAILLIART, B. Ribadeau‐Dumas
Journal of Food Science
Abstract
ABSTRACT Solubility of the main proteins in 10 x acid and rennet whey retentates was studied in the pH range 2.0 to 4.0 in the presence of NaCI from 2 to 15% (w/v) final concentration, at 20°C to find fractionation conditions suitable for preparing pure β‐lactoglobulin and β‐lactoglobu‐lin‐free whey proteins and scaling up. At pH 2.0, 7% NaCI, 20 min holding time, nearly all (3‐lactoglobulin remained soluble while a precipitate (PI) containing all other proteins was formed. Pure p‐lacto‐globulin was quantitatively recovered by salting‐out the centrifugation supernatant at 30% NaCI (w/v) final concentration. PI, insoluble at pHs lower than 4.0, was made soluble at any pH by dissolving at pH 9.0, dialyzing against 50 mM formic acid (pH 3.0) and freeze‐drying.
Extracted Claims
3 claims extracted from this paper into the knowledge graph
dialysis affects solubility of precipitate (PI) containing other whey proteins
“PI, insoluble at pHs lower than 4.0, was made soluble at any pH by dissolving at pH 9.0, dialyzing against 50 mM formic acid (pH 3.0) and freeze‐drying.”
NaCI salting out affects recovery of pure β-lactoglobulin
“Pure p‐lacto‐globulin was quantitatively recovered by salting‐out the centrifugation supernatant at 30% NaCI (w/v) final concentration.”
NaCI salting out affects solubility of β-lactoglobulin and other whey proteins
“At pH 2.0, 7% NaCI, 20 min holding time, nearly all (3‐lactoglobulin remained soluble while a precipitate (PI) containing all other proteins was formed.”