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Haloalkane dehalogenases: Biotechnological applications
Author(s) -
Koudelakova Tana,
Bidmanova Sarka,
Dvorak Pavel,
Pavelka Antonin,
Chaloupkova Radka,
Prokop Zbynek,
Damborsky Jiri
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.201100486
Subject(s) - bioremediation , biocatalysis , chemistry , protein engineering , biochemical engineering , cleave , combinatorial chemistry , pollutant , context (archaeology) , enzyme , biochemistry , organic chemistry , catalysis , biology , bacteria , reaction mechanism , paleontology , genetics , engineering
Haloalkane dehalogenases (EC 3.8.1.5, HLDs) are α/β‐hydrolases which act to cleave carbon‐halogen bonds. Due to their unique catalytic mechanism, broad substrate specificity and high robustness, the members of this enzyme family have been employed in several practical applications: (i) biocatalytic preparation of optically pure building‐blocks for organic synthesis; (ii) recycling of by‐products from chemical processes; (iii) bioremediation of toxic environmental pollutants; (iv) decontamination of warfare agents; (v) biosensing of environmental pollutants; and (vi) protein tagging for cell imaging and protein analysis. This review discusses the application of HLDs in the context of the biochemical properties of individual enzymes. Further extension of HLD uses within the field of biotechnology will require currently limiting factors – such as low expression, product inhibition, insufficient enzyme selectivity, low affinity and catalytic efficiency towards selected substrates, and instability in the presence of organic co‐solvents – to be overcome. We propose that strategies based on protein engineering and isolation of novel HLDs from extremophilic microorganisms may offer solutions.