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Gel properties of myofibrillar proteins heated at different heating rates under a low-frequency magnetic field.
Food Chemistry ( IF 8.8 ) Pub Date : 2020-04-02 , DOI: 10.1016/j.foodchem.2020.126728
Xian Wang 1 , Minquan Xia 1 , Yuanhua Zhou 2 , Limei Wang 1 , Xiaolong Feng 1 , Kun Yang 1 , Jing Ma 1 , Zhenshun Li 1 , Lan Wang 3 , Weiqing Sun 1
Affiliation  

The effects of low-frequency magnetic field combined with different heating rates on pork myofibrillar protein (MP) gels were investigated. Samples were treated under different heating rates (1 °C/min and 2 °C/min) in the presence or absence of 9.5 mT low-frequency magnetic field. The highest levels of intermolecular and intramolecular ionic and hydrogen bonds in MP were observed at the heating rate of 2 °C/min under the 9.5 mT magnetic field. These bonds resulted in decreasing the α-helix and increasing the β-sheet and β-turn, which promoted the formation of a more uniform microstructure. It also increased the proportion of bound water, increasing the ability of MP to bind with water. This effect, combined with the weaker hydrophobic interactions, as confirmed by the reduced content of tryptophan and aliphatic residues, explained well the high water-holding capacity of MP induced by heating at 2 °C/min under the 9.5 mT magnetic field.

中文翻译:

在低频磁场下以不同加热速率加热的肌原纤维蛋白的凝胶特性。

研究了低频磁场和不同加热速率对猪肉肌原纤维蛋白(MP)凝胶的影响。在存在或不存在9.5 mT低频磁场的情况下,以不同的加热速率(1°C / min和2°C / min)对样品进行处理。在9.5 mT磁场下以2°C / min的加热速率观察到MP中分子间和分子内离子和氢键的最高水平。这些键导致α-螺旋的减少和β-折叠和β-转角的增加,从而促进了更均匀的微观结构的形成。它还增加了结合水的比例,提高了MP与水结合的能力。色氨酸和脂肪族残基含量降低证实了这种效应,加上较弱的疏水作用,
更新日期:2020-04-03
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