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Investigation of Interaction Between Casein Enzyme Hydrolysate and Biosynthesized Silver Nanoparticles by Spectroscopy

机译:光谱法研究酪蛋白酶解产物与生物合成的银纳米粒子的相互作用

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摘要

The interaction between silver nanoparticles and casein enzyme hydrolysate-Type I have been carried out by spectroscopic techniques (fluorescence, UV-Visible, and circular dichroism) at different temperatures (293, 303 and 313 K). UV-Vis spectroscopic data suggested the formation of ground state complex between casein enzyme hydrolysate and silver nanoparticles. The silver nanoparticles have a strong ability to quench the intrinsic fluorescence of casein enzyme hydrolysate by quenching mechanisms through dynamic quenching process. The number of binding sites 'n' and binding constants 'K' were determined at different temperatures based on fluorescence quenching. The thermodynamic parameters (Delta H, Delta G, and Delta S) of the interaction system were calculated at different temperatures and the results suggested that the binding process was spontaneous and the acting force between casein enzyme hydrolysate and silver nanoparticles were mainly hydrophobic forces and electrostatic interaction. Based on the Forster non-radiation energy transfer theory, the average binding distance between casein enzyme hydrolysate and silver nanoparticles was estimated to be 4.67 nm. Both synchronous fluorescence and circular dichroism spectra confirmed the interaction as mentioned which reflected in the conformational change of casein enzyme in presence of silver nanoparticles.
机译:银纳米颗粒和I型酪蛋白酶水解产物之间的相互作用已通过光谱技术(荧光,紫外可见和圆二色性)在不同温度(293、303和313 K)下进行。 UV-Vis光谱数据表明酪蛋白酶水解物和银纳米颗粒之间形成了基态复合物。银纳米颗粒具有通过动态猝灭过程的猝灭机理猝灭酪蛋白酶水解产物的固有荧光的强大能力。基于荧光猝灭在不同温度下确定结合位点“ n”的数目和结合常数“ K”。计算了在不同温度下相互作用体系的热力学参数(ΔH,Delta G和Delta S),结果表明结合过程是自发的,酪蛋白酶水解物与纳米银的作用力主要为疏水力和静电。相互作用。基于Forster非辐射能量转移理论,酪蛋白酶水解物与银纳米颗粒之间的平均结合距离估计为4.67 nm。同步荧光和圆二色性光谱均证实了所提及的相互作用,这反映了在存在银纳米颗粒的情况下酪蛋白酶的构象变化。

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