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Investigating the Role of Conformational Effects on Laccase Stability and Hyperactivation under Stress Conditions.

Authors :
Ferrario V
Chernykh A
Fiorindo F
Kolomytseva M
Sinigoi L
Myasoedova N
Fattor D
Ebert C
Golovleva L
Gardossi L
Source :
Chembiochem : a European journal of chemical biology [Chembiochem] 2015 Nov 02; Vol. 16 (16), pp. 2365-72. Date of Electronic Publication: 2015 Oct 16.
Publication Year :
2015

Abstract

Fungal laccase from Steccherinum ochraceum 1833 displays remarkable stability under different harsh conditions: organic/buffer mixtures, thermal treatment, and microwave radiation. The behavior is particularly significant in the light of the sharp inactivation observed for two different fungal laccases. Laccase from S. ochraceum 1833 also displays hyperactivation under mild thermal treatment (60 °C). Molecular dynamics simulations at 80 °C explained how this laccase retains the geometry of the electron transfer pathway, thereby assuring electron transfer through the copper ions and thus maintaining its catalytic activity at high temperature. Spectroscopic studies revealed that the thermal activation corresponds to specific conformational changes in the protein. The results indicate that this laccase is potentially applicable under denaturing conditions that might be beneficial for the biotransformation of recalcitrant substrates.<br /> (© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Details

Language :
English
ISSN :
1439-7633
Volume :
16
Issue :
16
Database :
MEDLINE
Journal :
Chembiochem : a European journal of chemical biology
Publication Type :
Academic Journal
Accession number :
26360132
Full Text :
https://doi.org/10.1002/cbic.201500339