中华医学超声杂志

应用化学 ›› 2010, Vol. 27 ›› Issue (01): 96-101.

• 研究论文 • 上一篇    下一篇

PEG、TEPA与淀粉酶相互作用荧光光谱研究

王峰1*,梁力曼2,顾正彪3,崔正刚1   

  1. (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)
  • 收稿日期:2009-01-13 修回日期:2009-04-22 出版日期:2010-01-10 发布日期:2010-01-10
  • 通讯作者: 王峰，男，博士，副教授; E-mail:fwang@jiangnan.edu.cn; 研究方向：生化反应工程
  • 基金资助:
    国家高技术研究发展计划（“八六三”计划2006AA10Z335）资助项目

Fluorescent Spectrometry of Interaction of Amylase with Polyvinyl Alcohol and Polyethylenamnie

WANG Feng1*, LIANG Li-Man2, GU Zheng-Biao3, CUI Zheng-Gang1   

  1. (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)
  • Received:2009-01-13 Revised:2009-04-22 Published:2010-01-10 Online:2010-01-10

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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

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.

Key words: PEG, TEPA, amylase, interaction

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