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Purification of Glycomacropeptide from Caseinate Hydrolysate by Gel Chromatography and Treatment with Acidic Solution
Author(s) -
Nakano T.,
Ozimek L.
Publication year - 2000
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.1365-2621.2000.tb16054.x
Subject(s) - hydrolysate , chemistry , chromatography , biochemistry , hydrolysis
Glycomacropeptide (GMP) was purified from chymosin‐hydrolyzed caseinate solution by the procedure involving: (1) gel chromatography on Sephacryl S‐200 at pH 7.0 to obtain a crude GMP fraction; (2) addition of acidic solution, pH 3.5 to the crude glycomacropeptide to precipitate contaminating protein and/or peptide; and (3) re‐chromatography of the material soluble in the acidic solution on Sephacryl S‐200 at pH 3.5. The purified GMP accounted for 5.3% of dry weight of caseinate hydrolysate, and 0.7% of dry weight of sodium caseinate powder. The preparation was of considerably high purity with its amino‐acid composition showing only traces (each < 1 residue / peptide) of arginine, histidine, phenylalanine, and tyrosine, the amino acids that do not occur in GMP.