Affinity chromatography matrices for depletion and purification of casein glycomacropeptide from bovine whey

MARÍA FERNANDA BAIELI; NICOLÁS URTASUN; MARÍA JULIA MARTÍNEZ; DANIELA BELÉN HIRSCH; ANA MARÍA RENATA PILOSOF; MARÍA VICTORIA MIRANDA; OSVALDO CASCONE; FEDERICO JAVIER WOLMAN

BIOTECHNOLOGY PROGRESS

AMER CHEMICAL SOC

Lugar: Washington; Año: 2017 vol. 33 p. 171 - 180

8756-7938

Caseinglycomacropeptide (CMP) is a 64- amino acid peptide found in cheese whey, whichis released after κ-casein specific cleavage by chymosin. CMP lacks aromaticamino acids, a characteristic that makes it usable as a nutritional supplementfor people with phenylketonuria. CMP consists of two nonglycosylated isoforms(aCMP A and aCMP B) and its different glycosylated forms (gCMP A and gCMP B).The most predominant carbohydrate of gCMP is N-acetylneuraminic acid (sialicacid). Here, we developed a CMP purification process based on the affinity ofsialic acid for wheat germ agglutinin (WGA). After formation of chitosan beadsand adsorption of WGA, the agglutinin was covalently attached withglutaraldehyde. Two matrices with different WGA density were assayed for CMPadsorption. Maximum adsorption capacities were calculated according to theLangmuir model from adsorption isotherms developed at pH 7.0, being 137.0 mg/gfor the matrix with the best performance. In CMP reduction from whey, maximumremoval percentage was 79% (specifically 33.7% of gCMP A and B, 75.8% of aCMPA, and 93.9% of aCMP B). The CMP was recovered as an aggregate with an overallyield of 64%. Therefore, the matrices developed are promising for CMPpurification from cheese whey.