Oral tribology, adsorption and rheology of alternative food proteins
Oral tribology, adsorption and rheology of alternative food proteins
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DOI：
10.1016/j.foodhyd.2021.106636
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发表时间：
2021-02-18
影响因子：
10.7
通讯作者：
Sarkar, Anwesha
中科院分区：
文献类型：
--
作者：
Kew, Ben;Holmes, Melvin;Sarkar, Anwesha
使用摩擦学和吸附的机械知识可能有助于筛选具有更好润滑性的各种蛋白质;有助于快速跟踪用于低脂/高蛋白食品开发的新成分配方。本研究的目的是比较的润滑，吸附和物理化学性质的替代蛋白质（豌豆，马铃薯，羽扇豆和昆虫蛋白）与乳清分离蛋白（WPI）作为对照。选择豌豆蛋白质浓缩物（PPCsol）、昆虫蛋白质浓缩物（IPCsol）、马铃薯蛋白质分离物（PoPIsol）和羽扇豆蛋白质分离物（LPIsol）的可溶性级分（1-10重量%）作为替代蛋白质。所有蛋白质在中性pH下均带负电荷，并显示出不同程度的聚集（流体动力学直径范围为PoPIsol的25 nm至PPCsol的244 nm）。在5wt%蛋白质下的边界摩擦系数（mu）遵循PPCsol > LPIsol > IPCsol > PoPIsol > WPIsol的趋势，突出了PoPIsol、IPCsol和WPIsol的优异润滑性能。在较高的蛋白质浓度（10重量%）下，LPIsol、PoPIsol和IPCsol的mu显著增加，而WPIsol的mu降低。石英晶体微天平与耗散监测（QCM-D）的结果显示，形成刚性弹性膜的疏水表面上的PoPISol和WPISol引起低-而更粘的膜PPCsol导致高-。PPCsol具有最高的水合质量（11.0 mg m（-2）），与WPI sol（8.0 mg m（-2））相比，其他蛋白质的水合质量值较低（5.0-5.4 mg m（-2））。强烈的相关性之间存在的亩缩放到粘度，尺寸和水合质量和粘弹性的替代蛋白质的膜，验证摩擦响应中的表面连接的现象。
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.