中文摘要：

研究了经不同浓度盐酸胍变性的α-淀粉酶（α-Amylase）在疏水作用色谱（HIC）中的保留行为.结果表明,天然及经盐酸胍变性的α-淀粉酶在HIC中的保留行为都很好地遵循非线性Van′t Hoff方程,且由所计算出的α-淀粉酶在HIC中保留的热力学参数发现,在实验温度范围内,α-淀粉酶的保留为熵驱动,焓变（ΔH0）、熵变（ΔS0）和热容量变（ΔCP0）3个热力学参数都分别与绝对温度及其倒数之间存在线性关系.同时,对部分胍变α-淀粉酶的折叠自由能ΔΔGF进行了测定,发现变性α-淀粉酶在HIC固定相表面的折叠自由能远比在溶液中的高,且对于相同浓度盐酸胍变性的α-淀粉酶,均以298K时的折叠自由能为最大.

英文摘要：

The retention behavior for the denatured a-Amylase in hydrophobic interaction chromatography （HIC） was investigated. The results showed that the retention behaviors for a-Amylase were all well followed the non-linear Van＇t Hoff equation. The calculated thermodynamic parameters in retention of a-Amylase showed that the retention of a-Amylase in HIC is driven by entropy, and △H^0, △S^0 and △Cp^0 linearly correlate both with the corresponding absolute temperatures and their reciprocals, respectively. The calculated folding free energy △△GF 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.