β-半乳糖苷酶的动态光散射研究：环境对蛋白质构象和酶活性的影响

A dynamic light scattering study of beta-galactosidase: environmental effects on protein conformation and enzyme activity.

作者信息

Yang S T, Marchio J L, Yen J W

机构信息

Department of Chemical Engineering, Ohio State University, Columbus 43210.

出版信息

Biotechnol Prog. 1994 Sep-Oct;10(5):525-31. doi: 10.1021/bp00029a011.

DOI:10.1021/bp00029a011

PMID:7765378

Abstract

Dynamic light scattering (DLS) is a useful technique for analyzing the size, shape, and other structural characteristics of protein molecules in solution. The effects of various environmental conditions on the structure and activity of Aspergillus oryzae beta-galactosidase were studied. DLS was used to determine protein particle size under various salt, pH, and temperature conditions. Changes in the activity and stability of this enzyme caused by different environmental conditions were found to correlate well with the size changes of the protein particles. This change in protein size can be attributed to protein unfolding and aggregation under extreme conditions. The presence of the enzyme substrate, lactose, in the protein solution greatly enhanced enzyme stability by inhibiting aggregation.

摘要

动态光散射（DLS）是一种用于分析溶液中蛋白质分子大小、形状及其他结构特征的有用技术。研究了各种环境条件对米曲霉β-半乳糖苷酶结构和活性的影响。利用DLS测定了不同盐浓度、pH值和温度条件下的蛋白质颗粒大小。发现不同环境条件引起的该酶活性和稳定性变化与蛋白质颗粒大小变化密切相关。蛋白质大小的这种变化可归因于极端条件下蛋白质的展开和聚集。蛋白质溶液中酶底物乳糖的存在通过抑制聚集大大提高了酶的稳定性。