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The effectiveness of egg white protein and β-cyclodextrin during frozen storage: Functional, rheological and structural changes in the myofibrillar proteins of Culter alburnus
Food Hydrocolloids ( IF 11.0 ) Pub Date : 2020-08-01 , DOI: 10.1016/j.foodhyd.2020.105842
Noman Walayat , Zhouyi Xiong , Hanguo Xiong , Helena M. Moreno , Qing Li , Asad Nawaz , Zhongli Zhang , Pengkai Wang , Nadia Niaz

Abstract This study focused on the effects of egg white protein (EWP) and β-cyclodextrin (βCD) mixture (3:1, EWP/βCD) at 0, 2, 4 and 6% concentrations on fish (Culter alburnus) myofibrillar proteins (MP) during 60 days of frozen storage (−18 °C) by analyzing functional, rheological and structural changes in MP and MP gels. After 60 days of storage, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy revealed a decrease in the MP α-helix content, and EWP/βCD addition improved the MP secondary structural properties by inhibiting protein aggregation induced by exposure of hydrophobic residues. Particularly, the 6% EWP/βCD treatment significantly decreased (P

中文翻译:

蛋清蛋白和 β-环糊精在冷冻储存过程中的有效性:白鲟肌原纤维蛋白的功能、流变学和结构变化

摘要 本研究的重点是蛋清蛋白 (EWP) 和 β-环糊精 (βCD) 混合物(3:1,EWP/βCD)在 0、2、4 和 6% 的浓度下对鱼类(Culter alburnus)肌原纤维蛋白的影响。 MP) 在 60 天的冷冻储存 (-18 °C) 期间通过分析 MP 和 MP 凝胶的功能、流变学和结构变化。储存 60 天后,圆二色性 (CD) 和傅里叶变换红外 (FTIR) 光谱显示 MP α-螺旋含量降低,并且 EWP/βCD 添加通过抑制疏水暴露诱导的蛋白质聚集来改善 MP 二级结构特性。残留物。特别是 6% EWP/βCD 处理显着降低(P
更新日期:2020-08-01
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