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Ca2+诱导的淀粉液化芽孢杆菌α-淀粉酶分子的生物活性和结构变化
引用本文:冀旭,边六交.Ca2+诱导的淀粉液化芽孢杆菌α-淀粉酶分子的生物活性和结构变化[J].高等学校化学学报,2013,34(11):2517.
作者姓名:冀旭  边六交
作者单位:西北大学生命科学学院, 西安 710069
基金项目:国家自然科学基金(批准号:21075097)资助.
摘    要:在研究Ca2+对淀粉液化芽孢杆菌α-淀粉酶分子生物活性影响的基础上, 采用荧光光谱法和傅里叶变换红外光谱法研究了Ca2+诱导的酶分子结构变化. 结果表明, 当溶液中Ca2+浓度低于25.0 mmol/L时, Ca2+对酶分子具有激活作用; 而当Ca2+浓度高于25.0 mmol/L时, Ca2+对酶分子的生物活性具有抑制作用. 在Ca2+诱导的淀粉液化芽孢杆菌α-淀粉酶分子结构变化过程中, 酶分子仅发生二级结构的变化, 并不涉及其三级结构. 当Ca2+对酶分子具有激活作用时, 酶分子中的无规卷曲结构及β-折叠结构的含量下降, 而α-螺旋结构及β-转角结构的含量上升; 而当Ca2+对酶分子生物活性具有抑制作用时, 酶分子中的α-螺旋结构及β-转角结构的含量下降, 而无规卷曲结构及β-折叠结构的含量上升.

关 键 词:淀粉液化芽孢杆菌α-淀粉酶  Ca2+  生物活性  二级结构  
收稿时间:2013-03-12

Bioactive Change and Structural Change of Bacillus Amyloliquefaciens α-Amylases Induced by Ca2+
JI Xu,BIAN Liu-Jiao.Bioactive Change and Structural Change of Bacillus Amyloliquefaciens α-Amylases Induced by Ca2+[J].Chemical Research In Chinese Universities,2013,34(11):2517.
Authors:JI Xu  BIAN Liu-Jiao
Institution:College of Life Science, Northwest University, Xi'an 710069, China
Abstract:Based on the effect of bivalent calcium ions(Ca2+) on the biological activity of Bacillus amyloliquefaciens α-amylases, the structural change of Bacillus amyloliquefaciens α-amylases induced by Ca2+ was studied via fluorescence spectroscopy and Fourier-transformation infrared spectroscopy. The results showed that when the concentration of Ca2+ in solution was below 25 mmol/L, the enzyme molecules could be activated by Ca\+2+ in solution, when the concentration of Ca2+ was over 25 mmol/L, the biological activity of enzyme molecules could be inhibited by Ca2+. In the structural change of Bacillus amyloliquefaciens α-amylases induced by Ca2+, only their secondary structures rather than their tertiary structures were involved; and when Ca2+ showed an activation effect to the bioactivity of the enzyme molecules, the contents of disorder structures and β-sheet structures in the enzyme molecules decreased, and the α-helix ones and the β-turn ones increased. Whereas when Ca2+ showed an inhibition effect to the bioactivity of the enzyme molecules, the α-helix structures and β-turn structures in the enzyme molecules decreased, and disorder ones and the β-sheet ones in the enzyme molecules increased.
Keywords:Bacillus amyloliquefaciens α-amylase  Ca2+  Biological activity  Secondary structure  
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