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Characterization of the interaction between hen egg white lysozyme and ovalbumin
Food Bioscience ( IF 5.2 ) Pub Date : 2020-06-09 , DOI: 10.1016/j.fbio.2020.100674
Yongguo Jin , Qi Zeng , Fang Geng , Meihu Ma

As two major proteins of egg white, the interaction between lysozyme (LYZ) and ovalbumin (OVA) has been studied. In the present research, the mechanism and kinetics of the interaction between LYZ and OVA were studied using several methods, including cyclic voltammetry (CV), dual polarization interferometry (DPI) and surface plasmon resonance (SPR), and the effect of their interaction on the activity of LYZ was investigated using a bacteriolytic activity assay. Cyclic voltammograms showed that there was an interaction between these two proteins. DPI results indicated that the interaction is a type of chimeric mode, and the KA and KD of the interaction were 498 and 2.01 × 10−3 mol/L, respectively, calculated from the fitting of the surface plasmon resonance curve. The bacteriolytic activity assay showed that the interaction between these two proteins reduced the bacteriolytic activity of LYZ.



中文翻译:

鸡蛋清溶菌酶与卵清蛋白相互作用的表征

作为蛋白的两种主要蛋白质,溶菌酶(LYZ)和卵清蛋白(OVA)之间的相互作用已得到研究。在本研究中,使用循环伏安法(CV),双极化干涉法(DPI)和表面等离振子共振(SPR)等几种方法研究了LYZ和OVA之间相互作用的机理和动力学,以及它们对相互作用的影响。 LYZ的活性用溶菌活性测定法研究。循环伏安图显示这两种蛋白质之间存在相互作用。DPI结果表明相互作用是一种嵌合模式,相互作用的K AK D分别为498和2.01×10 -3 mol / L,分别由表面等离振子共振曲线的拟合计算得出。溶菌活性测定表明这两种蛋白之间的相互作用降低了LYZ的溶菌活性。

更新日期:2020-06-09
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