Diverse effects of aqueous polar co-solvents on Candida antarctica lipase B
Autor: | Matteo Luigi Pennati, Valerio Ferrario, Antonino Natalello, Alberto Barbiroli, Stefania Brocca, Marina Lotti, Juergen Pleiss, Henrique F. Carvalho, Marco Mangiagalli |
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Přispěvatelé: | Mangiagalli, M, Carvalho, H, Natalello, A, Ferrario, V, Pennati, M, Barbiroli, A, Lotti, M, Pleiss, J, Brocca, S |
Rok vydání: | 2020 |
Předmět: |
Protein Conformation
Kinetics FIS/07 - FISICA APPLICATA (A BENI CULTURALI AMBIENTALI BIOLOGIA E MEDICINA) 02 engineering and technology Molecular Dynamics Simulation CALB Organic solvents (In)activation mechanisms Biochemistry Acetone Fungal Proteins 03 medical and health sciences chemistry.chemical_compound Structural Biology Organic chemistry Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Aqueous solution biology Chemistry Dimethyl sulfoxide Basidiomycota Methanol Water General Medicine Lipase 021001 nanoscience & nanotechnology biology.organism_classification BIO/10 - BIOCHIMICA Enzyme Biocatalysis Solvents Candida antarctica 0210 nano-technology |
Zdroj: | International journal of biological macromolecules. 150 |
ISSN: | 1879-0003 |
Popis: | Biocatalysis in mixtures of water and co-solvents represents an opportunity to expand the application of enzymes. However, in the presence of organic solvents, enzymes can undergo reversible inhibition, inactivation, or aggregation. In this work, we studied the effects of three co-solvents (methanol, acetone, and dimethyl sulfoxide - DMSO) on the function and structure of the recombinant Candida antarctica lipase B (rCALB), a widely used enzyme in biotechnological applications. The effects of co-solvents on rCALB were investigated by steady-state kinetics experiments, biophysical assays and by molecular dynamics simulations in the presence and upon incubation with the three co-solvents. Methanol and acetone were found to act as competitive inhibitors of rCALB and to promote its aggregation, whereas DMSO is a non-essential activator of rCALB. |
Databáze: | OpenAIRE |
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