Effect of low-frequency magnetic field on the gel properties of pork myofibrillar proteins

被引:128
作者
Guo, Juanjuan [1 ]
Zhou, Yuanhua [3 ]
Yang, Kun [1 ]
Yin, Xiaoli [1 ]
Ma, Jing [1 ]
Li, Zhenshun [1 ]
Sun, Weiqing [1 ,2 ]
Han, Minyi [4 ]
机构
[1] Yangtze Univ, Coll Life Sci, Jingzhou 434023, Hubei, Peoples R China
[2] Yangtze Univ, Jingchu Food Res & Dev Ctr, Jingzhou 434023, Hubei, Peoples R China
[3] Yangtze Univ, Sch Mech Engn, Jingzhou 434023, Hubei, Peoples R China
[4] Nanjing Agr Univ, Minist Educ, Key Lab Meat Proc & Qual Control, Nanjing 210095, Jiangsu, Peoples R China
基金
中国国家自然科学基金;
关键词
Myofibrillar protein; Gel property; Low-frequency magnetic field; Rheological property; Raman spectroscopy; Low-field nuclear magnetic resonance; HEAT-INDUCED GELATION; WATER-HOLDING CAPACITY; HIGH-PRESSURE; RHEOLOGICAL PROPERTIES; VOLATILE COMPOUNDS; CHEMICAL FORCES; ULTRASOUND; PARAMETERS; FILMS; PH;
D O I
10.1016/j.foodchem.2018.09.028
中图分类号
O69 [应用化学];
学科分类号
081704 ;
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 alpha-helices unfolded and beta-sheets, beta-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.
引用
收藏
页码:775 / 781
页数:7
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