肌原纤维
化学
流变学
色氨酸
拉曼光谱
强度(物理)
化学工程
分析化学(期刊)
色谱法
材料科学
生物化学
氨基酸
复合材料
量子力学
光学
物理
工程类
作者
Juanjuan Guo,Yuanhua Zhou,Kun Yang,Xiaoli Yin,Jing Ma,Zhenshun Li,Weiqing Sun,Minyi Han
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2018-09-11
卷期号:274: 775-781
被引量:165
标识
DOI:10.1016/j.foodchem.2018.09.028
摘要
This study aimed to investigate the effect of a low-frequency magnetic field (LF-MF; 0, 0.25, 0.5, and 1.4 mT) on the gel properties of pork myofibrillar protein (MP) and to explore potential mechanisms. The water-holding capacity (WHC) and rheological properties of MP gels treated at 0.5 mT were better than those from other treatments. The water mobility did not change significantly as intensity increased, while the ratios of immobilized water (PT21) and free water (PT22) significantly decreased and increased, respectively. This suggested that the effect of LF-MF on MP hydration might be related to the formation of water clusters. Raman spectra suggested that α-helices unfolded and β-sheets, β-turns, and random coils were formed in MP gels (from 0.25 to 1.4 mT). Furthermore, the intensities of characteristic peaks in the tryptophan and aliphatic residues band were highest at 0.5 mT, indicating that 0.5 mT was the optimum intensity for hydrophobic interactions.
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