蛋清
化学
吸附
表面张力
蛋白质吸附
化学工程
十二烷基硫酸钠
无规线圈
蛋白质聚集
扫描电子显微镜
粘度
聚丙烯酰胺
粒径
色谱法
材料科学
蛋白质二级结构
食品科学
高分子化学
有机化学
复合材料
生物化学
物理
工程类
物理化学
量子力学
作者
Kefei Chang,Wei Jiang,Jingbo Liu
标识
DOI:10.1016/j.foodhyd.2021.107241
摘要
The effect of conventional heat treatment and subcritical water (SW) treatment on the structure and foaming properties of egg white protein (EWP) were investigated. Compared with unheated EWP, SW treatment enhanced the foaming capacity by 3-fold and induced the transition from α-helix structure (from 29.8% to 13.6%) to β-sheet structure (from 18.2% to 26.2%) and random coil structures (from 39.7% to 46.3%). Meanwhile, heating at 90 and 120 °C both remarkably increased the surface hydrophobicity and aggregation of EWP. The particle size of EWP (unheated, heated at 90 and 120 °C) was 104.37 nm, 438.5 nm and 311.6 nm, respectively. Combined with the results of sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE) electrophoresis, we speculated that SW treatment could hydrolyze protein aggregates formed at 90 °C into small molecular weight aggregation. Scanning electron microscopy revealed that SW treatment could induce the surface of EWP rougher, looser and more fragile. The viscosity and surface tension proved that SW treatment could improve the flexibility of EWP. These were all beneficial to the protein adsorption at the air-water interface and enhancement of foaming capacity. It might be of great significance for us to re-recognize the influence of high temperature on the foaming properties of egg white protein.
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