Heat-induced aggregation kinetics of potato protein-Investigated by chromatography, calorimetry, and light scattering

被引：17
作者：
Andlinger, David J. [1 ]
Schrempel, Ulrich [1 ]
Hengst, Claudia [1 ]
Kulozik, Ulrich [1 ]
机构：
[1] Tech Univ Munich, Chair Food & Bioproc Engn, TUM Sch Life Sci, Weihenstephaner Berg 1, D-85354 Freising Weihenstephan, Germany
来源：
FOOD CHEMISTRY | 2022年 / 389卷
关键词：
Patatin; Arrhenius; Degree of denaturation; Dynamic light scattering; Thiol; Reaction kinetics; Pl a n t protei n; BETA-LACTOGLOBULIN; SOY PROTEIN; DENATURATION; PATATIN; PH; TEMPERATURE; FRACTIONATION; MODEL;
D O I：
10.1016/j.foodchem.2022.133114
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
In this study, the heat-induced aggregation behavior of patatin rich potato protein isolate (PPI) was investigated by reversed-phase high-pressure liquid chromatography (RP-HPLC), differential scanning calorimetry (DSC), and dynamic light scattering. It could be shown that aggregation already occurs at low temperatures, despite low degrees of unfolding. The unfolding temperature, determined by DSC, coincided with a change in the reaction kinetics, which is determined by the unfolding step below a critical temperature up to the point, where the proteins are completely unfolded. The reaction rate k as a function of the absolute temperature T is then determined by diffusion of unfolded proteins forming aggregates. This change can be visualized in the Arrhenius diagram by a change of the slope of the relationship k ~ 1/T. A change in pH from 7 to 6 shifted the critical temperature towards higher values and resulted in larger aggregate sizes, due to reduced electrostatic repulsion.
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页数：9
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