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Applied and Environmental Microbiology, May 2006, p. 3637-3645, Vol. 72, No. 5
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.5.3637-3645.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Isolation and Biochemical Characterization of Two Novel Metagenome-Derived Esterases

C. Elend,^1, C. Schmeisser,^1, C. Leggewie,² P. Babiak,³ J. D. Carballeira,⁴ H. L. Steele,¹ J.-L. Reymond,³ K.-E. Jaeger,² and W. R. Streit^1*

Biofilm Centre, AG Molekulare Enzymtechnologie, Universität Duisburg-Essen, Lotharstrasse 1, D-47057 Duisburg, Germany,¹ Institut für Molekulare Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich, D-52426 Jülich, Germany,² Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland,³ Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany⁴

Received 4 November 2005/ Accepted 7 February 2006

The metagenomes of uncultured microbial communities are rich sources for novel biocatalysts. In this study, esterase EstA3 was derived from a drinking water metagenome, and esterase EstCE1 was derived from a soil metagenome. Both esterases are approximately 380 amino acids in size and show similarity to ß-lactamases, indicating that they belong to family VIII of the lipases/esterases. EstA3 had a temperature optimum at 50°C and a pH optimum at pH 9.0. It was remarkably active and very stable in the presence of solvents and over a wide temperature and pH range. It is active in a multimeric form and displayed a high level of activity against a wide range of substrates including one secondary ester, 7-[3-octylcarboxy-(3-hydroxy-3-methyl-butyloxy)]-coumarin, which is normally unreactive. EstCE1 was active in the monomeric form and had a temperature optimum at 47°C and a pH optimum at pH 10. It exhibited the same level of stability as EstA3 over wide temperature and pH ranges and in the presence of dimethyl sulfoxide, isopropanol, and methanol. EstCE1 was highly enantioselective for (+)-menthylacetate. These enzymes display remarkable characteristics that cannot be related to the original environment from which they were derived. The high level of stability of these enzymes together with their unique substrate specificities make them highly useful for biotechnological applications.

C.E. and C.S. contributed equally to this work.

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