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Optimisation of the hydrolysis of goat milk protein for the production of ACE-inhibitory peptides

Published online by Cambridge University Press:  20 March 2013

Francisco Javier Espejo-Carpio*
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
Raúl Pérez-Gálvez
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
Emilia M Guadix
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
Antonio Guadix
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
*
*For correspondence; e-mail: fjespejo@ugr.es

Abstract

Goat milk protein was hydrolysed with subtilisin and trypsin. As input variables, temperature was assayed in the interval 45–70 °C for subtilisin and 30–55 °C for trypsin, while the enzyme-substrate ratio varied from 1 to 5%. The effect of the input variables on the degree of hydrolysis and ACE-inhibitory activity (output variables) was modelled by second order polynomials, which were able to fit the experimental data with deviations below 10%. The individual maximum values of the degree of hydrolysis and the ACE-inhibitory activity were found at conflicting conditions of temperature and enzyme-substrate ratio. Since such maximum values could not be reached simultaneously, a bi-objective optimisation procedure was undertaken, producing a set of non-inferior solutions that weighted both objectives.

Type
Research Article
Copyright
Copyright © Proprietors of Journal of Dairy Research 2013

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