College of Food Science, Northeast Agricultural University, Harbin 150030, PR China.
Agricultural College, Northeast Agricultural University, Harbin 150030, PR China.
Food Chem. 2019 Jul 1;285:296-304. doi: 10.1016/j.foodchem.2019.01.170. Epub 2019 Feb 1.
Dried egg white powders are used in many segments of the food industry in place of traditional liquid egg materials. Dry heating during the processing of these products plays an essential role in obtaining their excellent functionalities, which are associated with protein aggregation. The objective of this study was to understand the aggregation behaviour of ovalbumin (OVA), the major component of egg-white proteins, during dry heating at 75 °C for 21 days. The results indicated that OVA aggregation increased from 28.7 ± 1.23% to 57.5 ± 2.45% as the reaction time increased, resulting in the generation of insoluble aggregates that were often 1-100 nm in diameter. However, a few soluble OVA aggregates became insoluble precipitates as their morphology changed from long strands to denser networks after 15 days of heat treatment. Moreover, covalent bonds, hydrophobic interactions and electrostatic repulsion played important roles in the formation of the small aggregates.
干蛋清白粉在食品工业的许多领域被用作传统液体蛋原料的替代品。在这些产品的加工过程中，干热起着至关重要的作用，这与蛋白质聚集有关。本研究的目的是了解卵清白蛋白（OVA）在 75°C 下干燥加热 21 天过程中的聚集行为。结果表明，OVA 聚集度从 28.7±1.23%增加到 57.5±2.45%，随着反应时间的增加，形成了不溶性聚集体，其直径通常为 1-100nm。然而，一些可溶性 OVA 聚集体在经过 15 天的热处理后，其形态从长链变为更密集的网络，从而变成不溶性沉淀。此外，共价键、疏水相互作用和静电排斥在小聚集体的形成中起着重要作用。
