高压加速葡萄糖异构酶晶体的生长动力学

High-pressure acceleration of the growth kinetics of glucose isomerase crystals.

作者信息

Suzuki Yoshihisa, Sazaki Gen, Matsui Takuro, Nakajima Kazuo, Tamura Katsuhiro

机构信息

Department of Chemical Science and Technology, Faculty of Engineering, The University of Tokushima, 2-1 Minamijosanjima, Tokushima 770-8506, Japan.

出版信息

J Phys Chem B. 2005 Mar 3;109(8):3222-6. doi: 10.1021/jp046419j.

DOI:10.1021/jp046419j

PMID:16851344

Abstract

The growth and dissolution rates of glucose isomerase crystals ({1 0 1} face) were measured in situ at 0.1 and 100 MPa. From these data, we determined that the solubilities at 25 degrees C were C(e) = 3.1 +/- 0.9 and 2.6 +/- 0.5 mg mL(-1) at 0.1 and 100 MPa, respectively. At the same supersaturation of sigma = 2.5 (sigma identical with ln(C/C(e)), C = the concentration of glucose isomerase, C(e) = the solubility) and temperature (T = 25 degrees C), the growth rate under 100 MPa was 7.6 times larger than that under 0.1 MPa. This result shows, for the first time, a kinetic acceleration of the growth rates of protein crystals with increasing pressure. The growth rates vs sigma data fitted well with a two-dimensional nucleation growth model of a polynucleation type. The fitting results indicate that the acceleration is mainly due to the decrease in the molecular surface energy of the glucose isomerase crystal with pressure.

摘要

在0.1和100MPa下原位测量了葡萄糖异构酶晶体（{1 0 1}面）的生长和解溶速率。根据这些数据，我们确定在25℃时，0.1和100MPa下的溶解度分别为C(e)=3.1±0.9和2.6±0.5mg mL(-1)。在相同的过饱和度σ=2.5（σ=ln(C/C(e))，C=葡萄糖异构酶浓度，C(e)=溶解度）和温度（T=25℃）下，100MPa下的生长速率比0.1MPa下的大7.6倍。该结果首次表明，随着压力增加，蛋白质晶体的生长速率出现动力学加速。生长速率与σ数据与多成核类型的二维成核生长模型拟合良好。拟合结果表明，加速主要是由于葡萄糖异构酶晶体的分子表面能随压力降低所致。