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  Non-canonical amino acids as a useful synthetic biological tool for lipase-catalysed reactions in hostile environments

Acevedo-Rocha, C. G., Hoesl, M., Nehring, S., Royter, M., Wolschner, C., Wiltschi, B., et al. (2013). Non-canonical amino acids as a useful synthetic biological tool for lipase-catalysed reactions in hostile environments. Catalysis Science & Technology, (5). doi:10.1039/C3CY20712A.

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 Creators:
Acevedo-Rocha, Carlos G.1, 2, Author              
Hoesl, Michael3, Author              
Nehring, Sebastian3, Author
Royter, Marina4, Author
Wolschner, Christina3, Author              
Wiltschi, Birgit5, Author              
Antranikian, Garabed4, Author
Budisa, Nediljko3, Author              
Affiliations:
1Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445588              
2Philipps-Universität Marburg, Hans-Meerwein-Straße, 35032 Marburg, Germany, ou_persistent22              
3Berlin Institute of Technology, Department of Chemistry, Biocatalysis Group, Franklinstrasse 29, 10587 Berlin, Germany , ou_persistent22              
4Institute of Technical Microbiology, Kasernenstrasse 12, 21073 Hamburg, Germany , ou_persistent22              
5MPI for Polymer Research, Max Planck Society, ou_1309545              

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 Abstract: The incorporation of several non-canonical amino acids into the Thermoanaerobacter thermohydrosulfuricus lipase confers not only activity enhancement upon treatment with organic solvents (by up to 450%) and surfactants (resp. 1630%), but also protective effects against protein reducing (resp. 140%), alkylating (resp. 160%), and denaturing (resp.190%) agents as well as inhibitors (resp. 40%). This approach offers novel chemically diversified biocatalysts for hostile environments.

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Language(s): eng - English
 Dates: 2013-022013
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C3CY20712A
 Degree: -

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Title: Catalysis Science & Technology
  Other : Catal. Sci. Technol.
Source Genre: Journal
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Publ. Info: Cambridge : Royal Society of Chemistry
Pages: - Volume / Issue: (5) Sequence Number: - Start / End Page: - Identifier: ISSN: 2044-4753
CoNE: https://pure.mpg.de/cone/journals/resource/2044-4753