Marasmius scorodonius extracellular dimeric peroxidase - exploring its temperature and pressure stability.
Marasmius scorodonius extracellular dimeric peroxidase - exploring its temperature and pressure stability.
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Marasmius scorodonius 细胞外二聚过氧化物酶 - 探索其温度和压力稳定性。
DOI：
10.1016/j.bbapap.2009.03.015
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发表时间：
2009
期刊：
影响因子：
--
通讯作者：
H. Zorn
中科院分区：
文献类型：
--
作者：
Matthias Pühse;Renate T Szweda;Yingying Ma;C. Jeworrek;R. Winter;H. Zorn
研究了来自担子菌 Marasmius scorodonius 的罕见过氧化物酶 MsP1 的温度和压力依赖性稳定性和功能。为此，将一系列生物物理技术（DSC、荧光和 FTIR 光谱、小角 X 射线散射）与酶的酶学研究相结合。事实证明，二聚体 MsP1 不仅具有相当的热稳定性，而且还具有很强的耐压性，即在环境温度下可承受高达约 65°C 的温度和高达 8-10kbar 的压力。值得注意的是，MsP1 的活性增加了两倍，直到 ∼500 bar。在约 2 kbar 的压力下，酶活性仍与环境压力条件下一样高。荧光和 SAXS 数据显示，MsP1 在 500 bar 左右的压力下活性增加可能是由于轻微的结构变化，这可能会稳定酶促反应的过渡态。由于 MsP1 具有显着的高压稳定性，它可能是工业高压应用的一个有价值的工具。
The temperature and pressure dependent stability and function of MsP1, an uncommon peroxidase from the basidiomycetous fungus Marasmius scorodonius were investigated. To this end, a series of biophysical techniques (DSC, fluorescence and FTIR spectroscopy, small-angle X-ray scattering) were combined with enzymatic studies of the enzyme. The dimeric MsP1 turned out to be not only rather thermostable, but also highly resistant to pressure, i.e., up to temperatures of about 65 °C and pressures as high as 8–10 kbar at ambient temperatures. Remarkably, the activity of MsP1 increased by a factor of two until ∼500 bar. At about 2 kbar, the enzymatic activity was still as high as under ambient pressure conditions. As revealed by the fluorescence and SAXS data, the increased activity of MsP1 at pressures around 500 bar may result from slight structural changes, which might stabilize the transition state of the enzymatic reaction. Owing to this marked high pressure stability of MsP1, it may represent a valuable tool for industrial high pressure applications.