A New Isolation Method of Caseinoglycopeptide from Sweet Cheese Whey

¹ Laboratory of Animal Products Chemistry, College of Agriculture, Tohoku University, Miyagi, Sendai 981, Japan

Caseinoglycopeptides were isolated from sweet cheese whey by alcohol precipitation and ion-exchange chromatography after heat coagulation of whey protein. The most successful method for obtaining the highest yield was by heating 10% (wt/vol) whey solution at pH 6.0 for 1 h, followed by precipitation with cold ethyl alcohol (50% vol/vol). The caseinoglycopeptide was fractionated into sialo- and asialo-caseinoglycopeptides by peanut (Arachis hypogoea) lectin-affinity chromatography. Caseinoglycopeptides exhibited five peaks on reverse-phase HPLC, which were divided into the first peak of an asialo-caseinoglycopeptide and sialo-caseinoglycopeptide in the following four peaks. The ratio of asialo-caseinoglycopeptide in whole caseinoglycopeptide is approximately 10%. Asialo-caseinoglycopeptide also could be prepared from cheese whey acidified to pH 3.0 and heated for 1 h at 98°C. Sialic acid in caseinoglycopeptide was completely released by this treatment. The yield of caseinoglycopeptide was approximately 1.1 g from 100 g of cheese whey powder.

Key Words: caseinoglycopeptide • isolation • sweet cheese whey

Submitted on October 22, 1990
Accepted on April 26, 1991

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