Preheat-stabilized pea proteins with anti-aggregation properties

March 24, 2020


Preheat-stabilized pea proteins with anti-aggregation properties


Chao Wu, Jiamei Wang, Wuchao Ma, Yiru Cai, Tao Wang




International Journal of Biological Macromolecules


Solution stability of food proteins is a crucial factor determining their shelf-life and sensory properties; yet to obtain stable protein products such as beverages is generally challenged by the growing demand for non-additive foods. Here, we report a facile method stabilizing pea proteins (PPs) by a simple preheating process at a concentration below 4% (w/v) and a temperature >90 °C. Far ultraviolet circular dichroism, fluorescence spectra, together with light scattering analyses demonstrated that the PPs were unfolded and became crosslinked via exposed hydrophobic moieties and disulfide bonds, giving rise to the formation a stable spatio-temporal interconnected system that could withstand the initial nucleation of aggregations. In addition, for reheated samples treated at a sufficiently high concentration of 15% (w/v), rheological characterizations revealed decreased aggregation along with increased preheating temperature and decreased preheating concentration. The robust strategy, along with the stabilized PPs in this study, would give a strong insight into preparation of heat-stable proteins with a wide span of concentrations, which may serve the needs for protein-enriched ingredients and satisfy the demands for cost-effective protocols applied in food industry.




Circular dichroism, Chemical stability, Thermal stability, Secondary structure, Biochemistry