Comparison of three fungal laccases from Rigidoporus lignosus and Pleurotus ostreatus: correlation between conformation changes and catalytic activity.
The conformation changes in solution of three fungal laccases in different environmental conditions were examined by circular dichroism (CD) and electron paramagnetic resonance (EPR) spectroscopy. CD measurements indicate that the secondary structure of proteins depends slightly on the pH or ionic strength, though the presence of salt could interfere in the molecular recognition process between substrates and enzymes. The enzymes, however, are highly destabilized by prolonged exposure to low pH or high temperature. The observed unfolding of the proteins coincides with their inactivation and, in some cases, with precipitation. On the other hand, these conditions do not determine the disruption of the geometric arrangement of their metal centres, and this fact suggests that these centres represent the more stable core of the proteins.
Bonomo
R P
RP
Dipartimento di Scienze Chimiche, Università di Catania, Italy. rbonomo@dipchi.unict.it
Cennamo
G
G
Purrello
R
R
Santoro
A M
AM
Zappalà
R
R
D002384:Catalysis; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D042845:Laccase; D009994:Osmolar Concentration; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D020076:Pleurotus / Q000201:enzymology*; D020072:Polyporales / Q000201:enzymology*; D011487:Protein Conformation; D013696:Temperature
D010088:Oxidoreductases; D042845:Laccase