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PH-Dependent molecular weight changes of kappa-casein glycomacropeptide and its preparation by ultrafiltration

, : PH-Dependent molecular weight changes of kappa-casein glycomacropeptide and its preparation by ultrafiltration. Milchwissenschaft 48(4): 191-196

K-Casein glycomacropeptide (GMP) is a biologically active peptide released from K-casein by chymosin. Although the theoretical molecular weight (MW) of GMP was about 7 kDa, the apparent MW of GMP on gel filtration was changed depending on pH. The distribution of the apparent MW ranged from 20 to 50 kDa at pH 7, but from 10 to 30 kDa at pH 3.5. GMP was rejected at pH 6.5 with ultrafiltration (UF) membranes with MW cut off of 50 or 20 kDa, but was mostly permeated through the same UF membranes at pH 3.5. We developed a simple procedure using UF for isolating GMP from whey protein concentrate (WPC), taking the pH-dependent change in the apaprent MW into account. The WPC solution was subjected to UF and diafiltration under acidic conditions using UF membrane with MW cut off of 50 kDa. After the permeate was neutralized, the second UF with the same UF membrane was carried out to retain GMP in the retentate. A lyophilized GMP powder was recovered with 63% yield and 81% purity.


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