Investigating the Role of Conformational Effects on Laccase Stability and Hyperactivation under Stress Conditions. Issue 16 (16th October 2015)

• Record Type: Journal Article
• Authors: Ferrario, Valerio; Chernykh, Alexey; Fiorindo, Federica; Kolomytseva, Marina; Sinigoi, Loris; Myasoedova, Nina; Fattor, Diana; Ebert, Cynthia; Golovleva, Ludmila; Gardossi, Lucia
• Is Part Of: Chembiochem. Volume 16:Issue 16(2015)
• Page Start: 2365
• Page End: 2372
• Publication Date: 2015-10-16
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201500339
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Fungal laccase from <italic>Steccherinum ochraceum</italic> 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 <italic>S. ochraceum</italic> 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.</p> </abstract>