西安工程大学学报2009，Vol.23Issue(4)：71-78,8.
α-淀粉酶在疏水作用色谱中保留的热力学研究
Thermodynamics of retention for α-amylase in hydrophobic interaction chromatography
摘要
Abstract
The retention behavior for the denatured α-Amylase in hydrophobic interaction chromatography (HIC) was investigated. The results showed that the retention behaviors for α-Amylase were all well followed the non-linear Van′t Hoff equation. The calculated thermodynamic parameters in retention of α-Amylase showed that the retention of α-Amylase in HIC is driven by entropy, andΔH0, ΔS0 and ΔCP 0 linearly correlate both with the corresponding absolute temperatures and their reciprocals, respectively. The calculated folding free energy ΔΔGF of partially denatured α-Amylase on the stationary phase surface in HIC are much higher than that in solution, and the highest folding free energy is at 298K.关键词
α-淀粉酶/疏水作用色谱/折叠自由能/热力学Key words
α-Amylase(α-Amy)/hydrophobic interaction chromatography (HIC)/folding free energy/thermodynamics分类
化学化工引用本文复制引用
冯小艳,耿信鹏,戴丽,吴丹,郑长征,耿信笃..α-淀粉酶在疏水作用色谱中保留的热力学研究[J].西安工程大学学报,2009,23(4):71-78,8.基金项目
Supported by the National Natural Science Foundation of China(20673080) （20673080）
