Quantification of protein-protein interactions in highly denatured whey and potato protein gels

Caren Tanger; David J Andlinger; Annette Brümmer-Rolf; Julia Engel; Ulrich Kulozik

doi:10.1016/j.mex.2021.101243

Quantification of protein-protein interactions in highly denatured whey and potato protein gels

MethodsX. 2021 Jan 26:8:101243. doi: 10.1016/j.mex.2021.101243. eCollection 2021.

Authors

Caren Tanger¹, David J Andlinger¹, Annette Brümmer-Rolf¹, Julia Engel¹, Ulrich Kulozik¹

Affiliation

¹ Chair for Food and Bioprocess Engineering, Technical University of Munich, Weihenstephaner Berg 1, Freising, Bavaria 85354, Germany.

Abstract

Understanding the stabilizing protein interactions in protein gels is of high importance for food- and biotechnology. Protein interactions in protein gels can help to predict hardness, deformability and other gel parameters. Currently there are two types methods used. One is to use protein interaction blocking agents and the other is to dissolve the gel in different buffer systems, which cleave the interactions. The first method alters the gelling mechanism, which is why the second method is the preferred one. However, currently published methods are often only suitable for specific gel systems as for example weakly bound protein gels. In this paper, a method is introduced, which is suitable for highly denatured whey and plant protein.•Suitable for strongly cross-linked whey protein and plant protein gels•Stronger buffer system to ensure cleavage of all protein interactions•More reproducible and simplified crushing of the gel without the introduction of uncontrolled shear stress excessively affecting the analysis of chemical bonds.

Keywords: Disulfide bonds; Dithiothreitol; Electrostatic interactions; Hydrophobic interactions; Sodium dodecyl sulfate; Solubility.