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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。

Gel properties of myofibrillar proteins heated at different heating rates under a low-frequency magnetic field.

机构信息

College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China.

School of Mechanical Engineering, Yangtze University, Jingzhou, Hubei 434023, PR China.

出版信息

Food Chem. 2020 Aug 15;321:126728. doi: 10.1016/j.foodchem.2020.126728. Epub 2020 Apr 2.

DOI:10.1016/j.foodchem.2020.126728
PMID:32259736
Abstract

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.

摘要

研究了低频磁场与不同升温速率对猪肉肌原纤维蛋白(MP)凝胶的影响。样品在不同的升温速率(1°C/min 和 2°C/min)下进行处理,有无 9.5mT 低频磁场。在 9.5mT 磁场下,升温速率为 2°C/min 时,MP 中分子间和分子内离子和氢键水平最高。这些键导致α-螺旋减少,β-折叠和β-转角增加,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,增加了 MP 与水结合的能力。这种效应,结合较弱的疏水性相互作用,如色氨酸和脂肪族残基含量的减少所证实的,很好地解释了在 9.5mT 磁场下以 2°C/min 的升温速率加热时 MP 高持水性的原因。

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