【摘 要】
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The rice glutelin(RG)solubility,surface hydrophobicity,intermolecular interaction of RG and amylose,binding parameters,binding force and conformational chan
【机 构】
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StateKeyLaboratoryofFoodScienceandTechnology,NanchangUniversity,Nanchang,Jiangxi,China
【出 处】
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2014年全国生物技术与食品质量博士后学术论坛
论文部分内容阅读
The rice glutelin(RG)solubility,surface hydrophobicity,intermolecular interaction of RG and amylose,binding parameters,binding force and conformational changes were investigated in RG-amylose mixed system.It was found that with the increasing of concentrations of amylose,solubility of RG was significantly increased accompanied with decreasing of surface hydrophobicity.The binding sites and the binding constant were calculated,and thermodynamic features indicating binding process was entropy-driven and spontaneous,with hydrophobic force was primarily responsible for their interaction.Furthermore,the microenvironment around the tyrosine residues and the secondary structure of RG were changed in the presence of amylose.In addition,a visual representation of two of the most energetically favorable binding sites located in the amorphous area of RG was presented by molecular modeling studies.
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