Diverse effects of aqueous polar co-solvents on Candida antarctica lipase B.
(In)activation mechanisms
CALB
Organic solvents
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 May 2020
01 May 2020
Historique:
received:
15
01
2020
revised:
11
02
2020
accepted:
14
02
2020
pubmed:
19
2
2020
medline:
5
1
2021
entrez:
19
2
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32068052
pii: S0141-8130(20)30334-2
doi: 10.1016/j.ijbiomac.2020.02.145
pii:
doi:
Substances chimiques
Fungal Proteins
0
Solvents
0
Water
059QF0KO0R
Acetone
1364PS73AF
Lipase
EC 3.1.1.3
lipase B, Candida antarctica
EC 3.1.1.3
Methanol
Y4S76JWI15
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
930-940Informations de copyright
Copyright © 2020. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest There are no conflicts of interest to declare.