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    Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions

    Kumagai, P.S. and Gutierrez, R.F. and Lopes, J.L.S. and Martins, J.M. and Jameson, D.M. and Castro, A.M. and Martins, L.F. and DeMarco, R. and Bossolan, N.R.S. and Wallace, Bonnie A. and Araujo, A.P.U. (2018) Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions. Extremophiles 22 (5), pp. 781-793. ISSN 1431-0651.

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    Abstract

    The biotechnological and industrial uses of thermostable and organic solvent-tolerant enzymes are extensive and the investigation of such enzymes from microbiota present in oil reservoirs is a promising approach. Searching sequence databases for esterases from such microbiota, we have identified in silico a potentially secreted esterase from Acetomicrobium hydrogeniformans, named AhEst. The recombinant enzyme was produced in E. coli to be used in biochemical and biophysical characterization studies. AhEst presented hydrolytic activity on short-acyl-chain p-nitrophenyl ester substrates. AhEst activity was high and stable in temperatures up to 75 °C. Interestingly, high salt concentration induced a significant increase of catalytic activity. AhEst still retained ~ 50% of its activity in 30% concentration of several organic solvents. Synchrotron radiation circular dichroism and fluorescence spectroscopies confirmed that AhEst displays high structural stability in extreme conditions of temperature, salinity, and organic solvents. The enzyme is a good emulsifier agent and is able to partially reverse the wettability of an oil-wet carbonate substrate, making it of potential interest for use in enhanced oil recovery. All the traits observed in AhEst make it an interesting candidate for many industrial applications, such as those in which a significant hydrolytic activity at high temperatures is required.

    Metadata

    Item Type: Article
    Additional Information: The final publication is available at Springer via the link above.
    Keyword(s) / Subject(s): Esterase, Protein stability, Synchrotron radiation circular dichroism (SRCD), spectroscopy, Fluorescence spectroscopy, Enhanced oil recovery (EOR)
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 19 Oct 2018 07:44
    Last Modified: 18 Nov 2019 17:32
    URI: http://eprints.bbk.ac.uk/id/eprint/24766

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