ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
: 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.2000.tb16054.x
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