Heat-induced lupin-whey protein emulsion-filled gels: Microstructural and rheological insights

TY - JOUR

T1 - Heat-induced lupin-whey protein emulsion-filled gels

T2 - Microstructural and rheological insights

AU - Grasberger, Katherine

AU - Vuholm Sunds, Anne

AU - Hammershøj, Marianne

AU - Corredig, Milena

N1 - Publisher Copyright: © 2024 The Authors

PY - 2024/6

Y1 - 2024/6

N2 - This work investigates the rheological properties of lupin-whey emulsion-filled gels (EFGs) formed using a pilot scale plate heat exchanger. Samples were prepared with either lupin, whey, or a lupin-whey stabilized emulsion, mixed in a whey protein continuous phase. While whey protein in the continuous phase was mainly responsible for the formation of a primary gel network, differences were observed depending on the droplet-whey protein matrix interactions. Full or partial replacement of interfacial proteins with lupin proteins resulted in softer, more ductile gels. Amplitude sweeps showed that the structure was not only affected by the interactions between the droplets and the continuous network, but also by the droplet distribution within the matrix. This work demonstrates the importance of fine tuning the interactions and the distribution of oil droplets within the gel, as these properties will lead to structural heterogeneity at the micro-scale, causing profound differences in the rheological properties. Finally, continuous heating led to stiffer, more particulate gels compared to quiescent conditions, but similar mechanisms underpinned gel formation. Thus, it is demonstrated that the design of the interactions can be screened using an in situ rheometer, although the rheological properties are affected by the shear effect of the plate heat exchanger.

AB - This work investigates the rheological properties of lupin-whey emulsion-filled gels (EFGs) formed using a pilot scale plate heat exchanger. Samples were prepared with either lupin, whey, or a lupin-whey stabilized emulsion, mixed in a whey protein continuous phase. While whey protein in the continuous phase was mainly responsible for the formation of a primary gel network, differences were observed depending on the droplet-whey protein matrix interactions. Full or partial replacement of interfacial proteins with lupin proteins resulted in softer, more ductile gels. Amplitude sweeps showed that the structure was not only affected by the interactions between the droplets and the continuous network, but also by the droplet distribution within the matrix. This work demonstrates the importance of fine tuning the interactions and the distribution of oil droplets within the gel, as these properties will lead to structural heterogeneity at the micro-scale, causing profound differences in the rheological properties. Finally, continuous heating led to stiffer, more particulate gels compared to quiescent conditions, but similar mechanisms underpinned gel formation. Thus, it is demonstrated that the design of the interactions can be screened using an in situ rheometer, although the rheological properties are affected by the shear effect of the plate heat exchanger.

KW - Emulsion-filled gels

KW - Food emulsions

KW - Lupin protein

KW - Plant-dairy protein mixtures

KW - Whey protein

U2 - 10.1016/j.lwt.2024.116269

DO - 10.1016/j.lwt.2024.116269

M3 - Journal article

AN - SCOPUS:85194418112

SN - 0023-6438

VL - 201

JO - LWT

JF - LWT

M1 - 116269

ER -