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Caseinomacropeptide behaviour in a whey protein fractionation process based on α-lactalbumin precipitation

Published online by Cambridge University Press:  17 March 2011

Ayoa Fernández
Affiliation:
Department of Chemical Engineering and Environmental Technology, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain
Violeta Menéndez
Affiliation:
Department of Chemical Engineering and Environmental Technology, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain
Francisco A Riera*
Affiliation:
Department of Chemical Engineering and Environmental Technology, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain
Ricardo Álvarez
Affiliation:
Department of Chemical Engineering and Environmental Technology, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain
*
*For correspondence; e-mail: far@uniovi.es

Abstract

This work studied the behaviour of caseinomacropeptide (CMP) in a whey protein fractionation process based on the selective precipitation of α-lactalbumin (α-la) in an acid medium. Three different acids (hydrochloric, citric and lactic) and different operating conditions (protein concentration, temperature and pH) were considered to perform the precipitation step. Under the optimised precipitation conditions obtained for α-la (pH 4, 55°C, initial α-la concentration around 12 g/l) CMP presents quite similar behaviour to that observed for β-lactoglobulin (β-lg), namely remaining in the supernatant fraction. However, at a lower pH value (3·5) the amount of precipitated CMP increases up to 72% when citric acid is added. This behaviour could be due to the fact that CMP is close to its isoelectric point, which allows a supernatant fraction enriched in β-lg that is almost free from the rest of proteins in sweet whey.

Type
Research Article
Copyright
Copyright © Proprietors of Journal of Dairy Research 2011

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Footnotes

Dedicated to the memory of Professor José M. Concellón

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