Abstract

In this study, we investigated the gelation of WPI fibrils in the presence of bacterial cellulose (BC) microfibrils at pH 2 upon prolonged heating. Rheology and microstructure were investigated as a function of BC microfibril concentration. The presence of BC microfibrils did not influence the gelation dynamics and resulting overall structure of the WPI fibrillar gel. The storage modulus and loss modulus of the mixed WPI‐BC microfibril gels increased with increasing BC microfibril concentration, whereas the ratio between loss modulus and storage modulus remained constant. The WPI fibrils and BC microfibrils independently form two coexisting gel networks. Interestingly, near to the BC microfibrils more aligned WPI fibrils seemed to be formed, with individual WPI fibrils clearly distinguishable. The level of alignment of the WPI fibrils seemed to be dependent on the distance between BC microfibrils and WPI fibrils. This also is in line with our observation that with more BC microfibrils present, WPI fibrils are more aligned than in a WPI fibrillar gel without BC microfibrils. The large deformation response of the gels at different BC microfibril concentration and NaCl concentration is mainly influenced by the concentration of NaCl, which affects the WPI fibrillar gel structures, changing form linear fibrillar to a particulate gel. The WPI fibrillar gel yields the dominant contribution to the gel strength.

Highlights

  • The ability of proteins to form fibrils under certain conditions has been suggested as a generic feature to all proteins (Chiti & Dobson, 2006; Dobson, 2003)

  • The turbidity increases with increase in bacterial cellulose (BC) microfibril concentration due to the presence of thicker and long BC microfibril bundles (Kuijk et al, 2013)

  • In the presence of BC microfibrils, the whey protein isolate (WPI) forms a fibrillar gel consisting of linear fibrillar aggregates

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Summary

Introduction

The ability of proteins to form fibrils under certain conditions has been suggested as a generic feature to all proteins (Chiti & Dobson, 2006; Dobson, 2003). Whey protein is a class of proteins frequently studied for fibril formation (Kroes-Nijboer, Venema, & van der Linden, 2012). A commercial system used for this purpose is whey protein isolate (WPI), containing a mixture of various types of whey protein. It is mainly composed of beta-lactoglobulin (β-lg), alpha-lactalbumin (α-lac), and bovine serum albumin (BSA) (De Wit, 1998). Upon heating WPI at 80 °C at pH 2 and low ionic strength for several hours, β-lg was found to be the protein involved in fibril formation (Bolder, Hendrickx, Sagis, & Van der Linden, 2006a, 2006b; Bolder, Vasbinder, Sagis, & van der Linden, 2007). The fibrillar gels prepared from whey proteins by prolonged heating at pH 2

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