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Organic co‐solvents affect activity, stability and enantioselectivity of haloalkane dehalogenases
Author(s) -
Stepankova Veronika,
Damborsky Jiri,
Chaloupkova Radka
Publication year - 2013
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201200378
Subject(s) - chemistry , biocatalysis , ethylene glycol , solvent , tetrahydrofuran , dimethyl sulfoxide , organic chemistry , solvent effects , combinatorial chemistry , catalysis , ionic liquid
Haloalkane dehalogenases are microbial enzymes with a wide range of biotechnological applications, including biocatalysis. The use of organic co‐solvents to solubilize their hydrophobic substrates is often necessary. In order to choose the most compatible co‐solvent, the effects of 14 co‐solvents on activity, stability and enantioselectivity of three model enzymes, DbjA, DhaA, and LinB, were evaluated. All co‐solvents caused at high concentration loss of activity and conformational changes. The highest inactivation was induced by tetrahydrofuran, while more hydrophilic co‐solvents, such as ethylene glycol and dimethyl sulfoxide, were better tolerated. The effects of co‐solvents at low concentration were different for each enzyme‐solvent pair. An increase in DbjA activity was induced by the majority of organic co‐solvents tested, while activities of DhaA and LinB decreased at comparable concentrations of the same co‐solvent. Moreover, a high increase of DbjA enantioselectivity was observed. Ethylene glycol and 1,4‐dioxane were shown to have the most positive impact on the enantioselectivity. The favorable influence of these co‐solvents on both activity and enantioselectivity makes DbjA suitable for biocatalytic applications. This study represents the first investigation of the effects of organic co‐solvents on the biocatalytic performance of haloalkane dehalogenases and will pave the way for their broader use in industrial processes.