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

Autor: Baieli MF; Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Biotecnología, Junín 956 (1113), Buenos Aires, Argentina.; Instituto de Nanobiotecnología (NANOBIOTEC), UBA, CONICET, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín, 956 (1113), Buenos Aires, Argentina., Urtasun N; Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Biotecnología, Junín 956 (1113), Buenos Aires, Argentina.; Instituto de Nanobiotecnología (NANOBIOTEC), UBA, CONICET, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín, 956 (1113), Buenos Aires, Argentina., Martinez MJ; Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Departamento de Industrias, Ciudad Universitaria (1428), Buenos Aires, Argentina., Hirsch DB; Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Biotecnología, Junín 956 (1113), Buenos Aires, Argentina.; Instituto de Nanobiotecnología (NANOBIOTEC), UBA, CONICET, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín, 956 (1113), Buenos Aires, Argentina., Pilosof AM; Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Departamento de Industrias, Ciudad Universitaria (1428), Buenos Aires, Argentina., Miranda MV; Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Biotecnología, Junín 956 (1113), Buenos Aires, Argentina.; Instituto de Nanobiotecnología (NANOBIOTEC), UBA, CONICET, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín, 956 (1113), Buenos Aires, Argentina., Cascone O; Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Biotecnología, Junín 956 (1113), Buenos Aires, Argentina.; Instituto de Nanobiotecnología (NANOBIOTEC), UBA, CONICET, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín, 956 (1113), Buenos Aires, Argentina., Wolman FJ; Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Biotecnología, Junín 956 (1113), Buenos Aires, Argentina.; Instituto de Nanobiotecnología (NANOBIOTEC), UBA, CONICET, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín, 956 (1113), Buenos Aires, Argentina.
Jazyk: angličtina
Zdroj: Biotechnology progress [Biotechnol Prog] 2017 Jan; Vol. 33 (1), pp. 171-180. Date of Electronic Publication: 2016 Nov 29.
DOI: 10.1002/btpr.2404
Abstrakt: Casein glycomacropeptide (CMP) is a 64- amino acid peptide found in cheese whey, which is released after κ-casein specific cleavage by chymosin. CMP lacks aromatic amino acids, a characteristic that makes it usable as a nutritional supplement for 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 (sialic acid). Here, we developed a CMP purification process based on the affinity of sialic acid for wheat germ agglutinin (WGA). After formation of chitosan beads and adsorption of WGA, the agglutinin was covalently attached with glutaraldehyde. Two matrices with different WGA density were assayed for CMP adsorption. Maximum adsorption capacities were calculated according to the Langmuir model from adsorption isotherms developed at pH 7.0, being 137.0 mg/g for the matrix with the best performance. In CMP reduction from whey, maximum removal percentage was 79% (specifically 33.7% of gCMP A and B, 75.8% of aCMP A, and 93.9% of aCMP B). The CMP was recovered as an aggregate with an overall yield of 64%. Therefore, the matrices developed are promising for CMP purification from cheese whey. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:171-180, 2017.
(© 2016 American Institute of Chemical Engineers.)
Databáze: MEDLINE
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