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    Oral tribology, adsorption and rheology of alternative food proteins

    Year: 2021

    Journal: Food Hydrocolloids, Volume 116, JUL

    Authors: Kew, Ben; Holmes, Melvin; Stieger, Markus; Sarkar, Anwesha

    Organizations: European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme [757993]

    Keywords: Friction; Plant protein; QCM-D; Viscosity; Sustainability; Insect protein

    Mechanistic knowledge using tribology and adsorption may help to screen various proteins with better lubrication; aiding the fast tracking of new ingredient formulations for use in low-fat/high protein food development. The aim of this study was to compare the lubrication, adsorption and physicochemical properties of alternative proteins (pea, potato, lupin and insect proteins) with whey protein isolate (WPI) as the control. Soluble fractions (1-10 wt%) of pea protein concentrate (PPCsol)(,) insect protein concentrate (IPCsol), potato protein isolate (PoPIsol) and lupin protein isolate (LPIsol) were chosen as the alternative proteins. All proteins were negatively charged at neutral pH and showed various degrees of aggregation (hydrodynamic diameters ranging from 25 nm for PoPIsol to 244 nm for PPCsol). The boundary friction coefficient (mu) at 5 wt% protein followed the trend as PPCsol > LPIsol > IPCsol > PoPIsol > WPIsol, highlighting excellent lubrication performances of PoPIsol, IPCsol and WPIsol. At higher protein concentrations (10 wt%), mu significantly increased for LPIsol, PoPIsol and IPCsol, while decreasing for WPIsol. Quartz crystal microbalance with dissipation monitoring (QCM-D) results revealed formation of rigid elastic films on hydrophobic surfaces by PoPIsol and WPIsol giving rise to low - while more viscous films by PPCsol led to high -. PPCsol had the highest hydrated mass (11.0 mg m(-2)) as compared to WPIsol(8.0 mg m(-2)) with lower values reported for other proteins (5.0-5.4 mg m(-2)). Strong correlations existed between mu scaled to viscosity, size and hydrated mass and viscoelasticity of films in alternative proteins, validating the surface-linked phenomena in frictional response.
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