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Comparison of selective hydrolysis of α-lactalbumin by acid Protease A and Protease M as alternative to pepsin: potential for β-lactoglobulin purification in whey proteins

Published online by Cambridge University Press:  07 February 2019

Katarina Lisak Jakopović*
Affiliation:
Laboratory for Technology of Milk and Milk products, Faculty of Food Technology and Biotechnology, University of Zagreb, Pierottijeva 6, HR-10000, Zagreb, Croatia
Seronei Chelulei Cheison
Affiliation:
Global Applied Science & Technology (GAST), Mars GmbH, Eitzerstr 215, D-27283 Verden (Aller), Germany
Ulrich Kulozik
Affiliation:
Chair for Food and Bioprocess Engineering, ZIEL Institute for Food & Health, Technical University of Munich, Weihenstephaner Berg 1, D-85354 Freising, Germany
Rajka Božanić
Affiliation:
Laboratory for Technology of Milk and Milk products, Faculty of Food Technology and Biotechnology, University of Zagreb, Pierottijeva 6, HR-10000, Zagreb, Croatia
*
Author for correspondence: Katarina Lisak Jakopović, Email: [email protected]

Abstract

The experiments reported in this research paper examine the potential of digestion using acidic enzymes Protease A and Protease M to selectively hydrolyse α-lactalbumin (α-La) whilst leaving β-lactoglobulin (β-Lg) relatively intact. Both enzymes were compared with pepsin hydrolysis since its selectivity to different whey proteins is known. Analysis of the hydrolysis environment showed that the pH and temperature play a significant role in determining the best conditions for achievement of hydrolysis, irrespective of which enzyme was used. Whey protein isolate (WPI) was hydrolysed using pepsin, Acid Protease A and Protease M by randomized hydrolysis conditions. Reversed-phase high performance liquid chromatography was used to analyse residual proteins. Regarding enzyme selectivity under various milieu conditions, all three enzymes showed similarities in the reaction progress and their potential for β-Lg isolation.

Type
Research Article
Copyright
Copyright © Hannah Dairy Research Foundation 2019 

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