Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation.
Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation.
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DOI：
10.1016/j.meatsci.2010.02.019
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发表时间：
2010-07
期刊：
影响因子：
7.1
通讯作者：
Xiufang Xia;B. Kong;Y. Xiong;Yanming Ren
中科院分区：
文献类型：
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作者：
Xiufang Xia;B. Kong;Y. Xiong;Yanming Ren
研究了冻融循环（FT、0、1、3 和 5 次）对猪最长肌蛋白质功能特性的影响。 FT 增加了肌纤维之间的间隙并撕裂肌纤维束。从 FT 肌肉中分离出的肌原纤维蛋白 (MP) 显示出疏水性增加 (P<0.05)、热转变温度 (Tmax) 和变性焓 (ΔH) (P<0.05) 降低以及对热聚集的敏感性增强。这些结构变化导致蛋白质功能的重大损失，例如，五个 FT 循环后，MP 乳化能力和乳液稳定性降低 41-43%（P<0.05）。通过小应变振荡流变测试分析，MP 形成粘弹性凝胶网络的能力也随着 FT 循环而减弱。 FT 过程降低了 MP 凝胶的持水能力 (WHC)、白度和质地（硬度、弹性、咀嚼性和内聚性）（P<0.05）。总体而言，重复的 FT 对猪 MP 的一般功能有不利影响，并且蛋白质变性和聚集与功能损失有关。
The effects of freeze–thaw cycles (FT, 0, 1, 3 and 5 times) on protein functional properties of porcine longissimus muscle were investigated. FT increased gapping between muscle fibres and tore muscle fiber bundles. Myofibrillar protein (MP) isolated from FT muscle showed an increased hydrophobicity (P<0.05), reduced thermal transition temperatures (Tmax) and enthalpy of denaturation (ΔH) (P<0.05), and enhanced susceptibility to thermal aggregation. These structural changes resulted in major losses in protein functionalities, e.g., 41–43% reductions (P<0.05) in MP emulsifying capacity and emulsion stability after five FT cycles. The ability of MP to form a viscoelastic gel network, as analyzed by small-strain oscillatory rheological testing, also attenuated with FT cycles. The FT process lowered (P<0.05) water-holding capacity (WHC), whiteness, and texture (hardness, springiness, chewiness and cohesiveness) of MP gels. Overall, repeated FT had a detrimental effect on the general functionality of porcine MP, and protein denaturation and aggregation were implicated in the functionality losses.