Abstract

The influence of thermomechanical treatment (temperature 60 °C–100 °C and shear rate 0.06 s−1–50 s−1) and mixing ratio of β-lactoglobulin (βLG) and α-lactalbumin (αLA) (5:2 and 1:1) on the denaturation and aggregation of whey protein model systems with a protein concentration of 60% and 70% (w/w) was investigated. An aggregation onset temperature was determined at approx. 80 °C for both systems (5:2 and 1:1 mixing ratio) with a protein concentration of 70% at a shear rate of 0.06 s−1. Increasing the shear rate up to 50 s−1 led to a decrease in the aggregation onset temperature independent of the mixing ratio. By decreasing the protein concentration to 60% in unsheared systems, the aggregation onset temperature decreased compared to that at a protein concentration of 70%. Furthermore, two significantly different onset temperatures were determined when the shear rate was increased to 25 s−1 and 50 s−1, which might result from a shear-induced phase separation. Application of combined thermal and mechanical treatment resulted in overall higher degrees of denaturation independent of the mixing ratio and protein concentration. At the conditions applied, the aggregation of the βLG and αLA mixtures was mainly due to the formation of non-covalent bonds. Although the proportion of disulfide bond aggregation increased with treatment temperature and shear rate, it was higher at a mixing ratio of 5:2 compared to that at 1:1.

Highlights

  • Extrusion processing has been used to produce functional whey protein-based emulsifiers and thickeners [1,2,3,4]

  • The results showed that a combination of thermal and mechanical treatment led to higher degrees of denaturation for all the protein systems investigated

  • The results showed that the shear stress influenced the denaturation reaction of βLG and αLA differently. These results show that the denaturation and aggregation kinetics known from diluted systems cannot be applied for highly concentrated systems

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Summary

Introduction

Extrusion processing has been used to produce functional whey protein-based emulsifiers and thickeners [1,2,3,4]. 30%) are treated simultaneously thermally and mechanically, which can lead to protein denaturation and the formation of structures consisting of aggregated proteins. Depending on the treatment conditions (thermal and mechanical stress profile, and milieu conditions), the globular protein structures unfold, new protein–protein interactions are formed, and aggregation takes place. Since the properties of the resulting aggregates (e.g., form, size, and stabilizing intermolecular interactions) play a crucial role in the functionality of the treated proteins [5], controlling the final product properties requires exact data on the reactions taking place (i.e., denaturation and aggregation). There is plenty of information about the effect of temperature and/or shear rate on the denaturation of whey

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