肌原纤维
化学
呋喃
Zeta电位
超声波
氢键
色谱法
疏水效应
溶解度
固相微萃取
质谱法
有机化学
生物化学
气相色谱-质谱法
分子
化学工程
纳米颗粒
物理
声学
工程类
作者
Xiaocao Zhao,Jun Qi,Chaoxia Fan,Bo Wang,Cong Yao,Dengyong Liu
出处
期刊:Food Chemistry
[Elsevier]
日期:2022-08-01
卷期号:384: 132472-132472
被引量:33
标识
DOI:10.1016/j.foodchem.2022.132472
摘要
This study was designed to explore the effects of different ultrasound power levels (0-600 W) on the ability of myofibrillar protein (MP) to bind furan compounds by analyzing the results of SDS-PAGE, particle size, Raman spectra, fluorescence intensity, solubility, turbidity, zeta potential, surface hydrophobicity, sulfhydryl content, solid-phase microextraction (SPME) and gas chromatography-mass spectrometry (GC-MS). As ultrasound power levels were increased from 0 to 500 W, the hydrophobic bonding sites, hydrogen-bonding sites, and electrostatic effects increased due to the unfolding and depolymerization of MP, thus enhancing the ability of MP to bind furan (flavor-enhancing) compounds. Consistent with these results, the positive effect of ultrasound resulted in ability of MP to bind furan compounds increased by 19.00 % to 33.32 %. However, after 600-W ultrasound treatment, the MP aggregated again and the bonding sites were re-embedded, which decreased the furan-binding ability.
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