| PEG、TEPA与淀粉酶相互作用荧光光谱研究 |
| |
| 引用本文： | 王峰,梁力曼,顾正彪,崔正刚.PEG、TEPA与淀粉酶相互作用荧光光谱研究[J].应用化学,2010,27(1):96-101. |
| |
| 作者姓名： | 王峰 梁力曼 顾正彪 崔正刚 |
| |
| 作者单位： | (1.江南大学化学与材料工程学院 无锡214122；2.河北科技师范学院化学系 秦皇岛；3.江南大学食品学院 无锡) |
| |
| 基金项目： | 国家高技术研究发展计划（“八六三”计划2006AA10Z335）资助项目 |
| |
| 摘 要： | 采用荧光光谱和紫外吸收光谱法研究聚乙烯醇(PEG)和四乙烯五胺(TEPA)与淀粉酶相互作用。 结果表明,PEG会增强淀粉酶内源性荧光和酪氨酸残基所处微环境的疏水性；TEPA对淀粉酶内源性荧光的猝灭机制属于动态猝灭，但同时也存在静态猝灭特征，并使色氨酸残基所处微环境的极性增大；在所考察的范围内， PEG与淀粉酶的结合常数在40 ℃达到最高，TEPA对淀粉酶荧光的动态猝灭结合常数在30 ℃以上趋于最大，PEG、TEPA与淀粉酶之间的作用力属于疏水与静电作用相结合。
|
| 关 键 词： | 聚乙烯醇 聚乙烯胺 淀粉酶 相互作用 |
| 收稿时间： | 2009-01-13 |
| 修稿时间： | 2009-04-22 |
Fluorescent Spectrometry of Interaction of Amylase with Polyvinyl Alcohol and Polyethylenamnie |
| |
| WANG Feng,LIANG Li-Man,GU Zheng-Biao,CUI Zheng-Gang.Fluorescent Spectrometry of Interaction of Amylase with Polyvinyl Alcohol and Polyethylenamnie[J].Chinese Journal of Applied Chemistry,2010,27(1):96-101. |
| |
| Authors: | WANG Feng LIANG Li-Man GU Zheng-Biao CUI Zheng-Gang |
| |
| Institution: | (1.School of Chemical and Meterial Engineering,Jiangnan University,Wuxi 214122;
2.Department of chemisty,Hebei Normal Universiy of Science and Technology,Qinhuangdao;
3.School of Food Science and Technolgy,Jiangnan University,Wuxi) |
| |
| Abstract: | Polyvinyl alcohol(PEG) and polyethylenamine(PEI) have been widely applied in the technological fields related to biochemistry. In this work, the interactions of amylase with PEG and tetraethylene pentamine(TEPA) were investigatied by fluorescence and UV absorption spectra. The results show both the inner fluorescence of amylase and the hydrophobicity of the microenvironment of tyrosine residues are enhanced in the presence of PEG. The quenching mechanism of inner fluorescence of amylase by TEPA is dynamic, but also exhibits a feature of static quenching. The polarity of microenvironment of tryptophan residues of amylase interacting with TEPA increases. In the range of this investigation, the binding constant of interaction of PEG with amylase reaches the highest value at 40 ℃, the value of quenching constant of binding between TEPA and amylase tends toward the maximum at 30 ℃. The interaction of amylse with PEG or TEPA involves hydrophobic and electrostatic interactions. |
| |
| Keywords: | PEG TEPA amylase interaction |
|
| 点击此处可从《应用化学》浏览原始摘要信息 |
| 点击此处可从《应用化学》下载免费的PDF全文 |
