Biology 2013, 2(1), 177-188; doi:10.3390/biology2010177

Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome

1 Laboratory of Biological Macromolecules, Centre for Protein Engineering, University of Liège, Institut de Chimie B6a, Liège, Sart-Tilman (4000), Belgium 2 Department of Earth System Science & Department of Ecology and Evolutionary Biology, University of California Irvine, 3208 Croul Hall, 92697 Irvine CA, USA 3 Puratos Group, Rue Bourrie 12, Andenne, Belgium 4 Puratos Group, Industrielaan 25, Groot-Bijgarden, Belgium 5 Department of Microbiology, Immunology and Biotechnology, School of Pharmacy and Biochemistry, University of Buenos Aires, Junin 956 (1113), Buenos Aires, Argentina These authors equally contributed to this work.
* Author to whom correspondence should be addressed.
Received: 3 December 2012; in revised form: 4 January 2013 / Accepted: 11 January 2013 / Published: 25 January 2013
(This article belongs to the Special Issue Polar Microbiology: Recent Advances and Future Perspectives)
PDF Full-text Download PDF Full-Text [513 KB, uploaded 25 January 2013 10:28 CET]
Abstract: An Antarctic soil metagenomic library was screened for lipolytic enzymes and allowed for the isolation of a new cytosolic esterase from the a/b hydrolase family 6, named MHlip. This enzyme is related to hypothetical genes coding esterases, aryl-esterases and peroxydases, among others. MHlip was produced, purified and its activity was determined. The substrate profile of MHlip reveals a high specificity for short p-nitrophenyl-esters. The apparent optimal activity of MHlip was measured for p-nitrophenyl-acetate, at 33 °C, in the pH range of 6–9. The MHlip thermal unfolding was investigated by spectrophotometric methods, highlighting a transition (Tm) at 50 °C. The biochemical characterization of this enzyme showed its adaptation to cold temperatures, even when it did not present evident signatures associated with cold-adapted proteins. Thus, MHlip adaptation to cold probably results from many discrete structural modifications, allowing the protein to remain active at low temperatures. Functional metagenomics is a powerful approach to isolate new enzymes with tailored biophysical properties (e.g., cold adaptation). In addition, beside the ever growing amount of sequenced DNA, the functional characterization of new catalysts derived from environment is still required, especially for poorly characterized protein families like α/b hydrolases.
Keywords: α/b hydrolase; lipolytic enzymes; metagenomics; p-nitrophenyl-ester; cold-adaptation

Article Statistics

Load and display the download statistics.

Citations to this Article

Cite This Article

MDPI and ACS Style

Berlemont, R.; Jacquin, O.; Delsaute, M.; La Salla, M.; Georis, J.; Verté, F.; Galleni, M.; Power, P. Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. Biology 2013, 2, 177-188.

AMA Style

Berlemont R, Jacquin O, Delsaute M, La Salla M, Georis J, Verté F, Galleni M, Power P. Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. Biology. 2013; 2(1):177-188.

Chicago/Turabian Style

Berlemont, Renaud; Jacquin, Olivier; Delsaute, Maud; La Salla, Marcello; Georis, Jacques; Verté, Fabienne; Galleni, Moreno; Power, Pablo. 2013. "Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome." Biology 2, no. 1: 177-188.

Biology EISSN 2079-7737 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert