Marasmius scorodonius extracellular dimeric peroxidase - exploring its temperature and pressure stability.
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 degrees C and pressures as high as 8-10 kbar at ambient temperatures. Remarkably, the activity of MsP1 increased by a factor of two until approximately 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.
Pühse
Matthias
M
Physical Chemistry I - Biophysical Chemistry, Dortmund University of Technology, D-44227 Dortmund, Germany.
Szweda
Renate T
RT
Ma
Yingying
Y
Jeworrek
Christoph
C
Winter
Roland
R
Zorn
Holger
H
D002152:Calorimetry, Differential Scanning; D019281:Dimerization; D004795:Enzyme Stability; D055433:Marasmius / Q000201:enzymology*; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*; D011312:Pressure; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D010544:Peroxidases