Hydrostatic Pressure Increases the Catalytic Activity of Amyloid Fibril Enzymes
Hydrostatic Pressure Increases the Catalytic Activity of Amyloid Fibril Enzymes
复制标题
DOI：
10.1002/anie.201605715
复制
发表时间：
2016-09-26
影响因子：
16.6
通讯作者：
Winter, Roland
中科院分区：
文献类型：
--
作者：
Trung Quan Luong;Erwin, Nelli;Winter, Roland
我们研究了压力（0.1-200 MPa）和温度（22，30，和38摄氏度）的组合效应的催化活性的设计淀粉样蛋白原纤维使用高压停流系统与快速UV/维斯吸收检测。互补的FT-IR光谱数据显示了显着高的压力和温度稳定性的原纤系统。由于在所有温度下的负活化体积（约-14 cm（3）mol（-1）），高压增强酯酶活性。这种增强在所覆盖的整个温度范围内持续，这允许在高温下进一步加速酶活性（活化能45-60 kJ mol（-1））。我们的数据揭示了使用压力和温度调制来优化催化淀粉样蛋白原纤维的酶效率的巨大潜力。
We studied the combined effects of pressure (0.1-200 MPa) and temperature (22, 30, and 38 degrees C) on the catalytic activity of designed amyloid fibrils using a high-pressure stopped-flow system with rapid UV/Vis absorption detection. Complementary FT-IR spectroscopic data revealed a remarkably high pressure and temperature stability of the fibrillar systems. High pressure enhances the esterase activity as a consequence of a negative activation volume at all temperatures (about -14 cm(3) mol(-1)). The enhancement is sustained in the whole temperature range covered, which allows a further acceleration of the enzymatic activity at high temperatures (activation energy 45-60 kJ mol(-1)). Our data reveal the great potential of using both pressure and temperature modulation to optimize the enzyme efficiency of catalytic amyloid fibrils.