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Preparation of β‐Lactoglobulin and p‐Lactoglobulin‐Free Proteins from Whey Retentate by NaCI Salting Out at Low pH
Author(s) -
MAILLIART P.,
RIBADEAUDUMAS B.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb08945.x
Subject(s) - chemistry , chromatography , solubility , beta lactoglobulin , isoelectric point , whey protein , formic acid , centrifugation , fractionation , diafiltration , dissolution , salting out , aqueous solution , biochemistry , organic chemistry , membrane , microfiltration , enzyme
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.