摘要
研究了乙基麦芽酚对胰α-淀粉酶活性的影响,以及二者相互作用的荧光猝灭光谱、同步荧光光谱和三维荧光光谱特征.证实了乙基麦芽酚对胰α-淀粉酶活性具有激活作用.证实了乙基麦芽酚与胰α-淀粉酶间的相互作用为静态猝灭,求出了猝灭常数以及乙基麦芽酚与胰α-淀粉酶的结合常数K和结合位点数n.由求得的热力学参数,根据Ross判断生物大分子和小分子结合力性质的规律推测,乙基麦芽酚与胰α-淀粉酶之间的作用力主要为疏水作用力.用同步荧光光谱和三维荧光光谱技术探讨了乙基麦芽酚对胰α-淀粉酶蛋白构象的影响.
The effect of ethyl maltol on the activity of α-amylas and the interaction feature of ethyl maltol and α-amylas was studied by fluorescence quenching spectra,synchronous fluorescence spectra and threedimensional fluorescence spectra.Treatment of α-amylas with ethyl maltol resulted in the activation function of α-amylas activity.It was proved that the quenching of Ethyl maltol on α-amylas was a static quenching process,the quenching constant K_q of a-amylas was obtained through stern-volmer plots and gained the binding constant of Ethyl maltol and the number of binding sites of Ethyl maltol.According to the thermodynamic equation and the criterion of assessing the type of interaction force bewteen biomacromolecule and biomicromolecule given by Ross,the interaction force between ethyl maltol and α- amylase was typical hydrophobic interactiones.The effect of ethyl maltol on the structure of α-amylas was analyzed by synchronous fluorescence spectra and three-dimensional fluorescence spectra.
出处
《四川大学学报（自然科学版）》
CAS
CSCD
北大核心
2009年第6期1870-1876,共7页
Journal of Sichuan University(Natural Science Edition)
