MULTI-FUNCTIONAL POLYMER SCAFFOLDS FOR CLEANING CATALYSIS
Lead Research Organisation:
University of Glasgow
Department Name: School of Life Sciences
Abstract
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People |
ORCID iD |
| Susan Rosser (Principal Investigator) |
Publications
Jensen MV
(2016)
Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain.
in PloS one
| Description | We engineered a range of esterase enzymes for attachment to chemical polymer scaffolds and demonstrated that the addition of attachment domains did not impact on their activities. |
| Exploitation Route | We have a range of active esterases engineered such that they can be attached to a range of chemistries including polymers and PEG modified surfaces. |
| Sectors | Agriculture, Food and Drink,Chemicals,Environment,Manufacturing, including Industrial Biotechology,Pharmaceuticals and Medical Biotechnology |
| Title | Datasets supporting "Characterisation of a New Family of Carboxyl Esterases with an OsmC domain" |
| Description | These data support the publication "Characterisation of a New Family of Carboxyl Esterases with an OsmC domain". Proteins in the serine esterase family are widely distributed in bacterial phyla and display activity against a range of biologically produced and chemically synthesized esters. A serine esterase from the psychrophilic bacterium Pseudoalteromonas arctica with a C-terminal OsmC-like domain was recently characterized; here we report on the identification and characterization of further putative esterases with OsmC-like domains constituting a new esterase family that is found in a variety of bacterial species from different environmental niches. All of these proteins contained the Ser-Asp-His motif common to serine esterases and a highly conserved pentapeptide nucleophilic elbow motif. We produced these proteins heterologously in Escherichia coli and demonstrate their activity against a range of esterase substrates. Two of the esterases characterized have activity of over two orders of magnitude higher than other members of the family, and are active over a wide temperature range. We determined the crystal structure of the esterase domain of the protein from Rhodothermus marinus and show that it conforms to the classical a/ß hydrolase fold with an extended 'lid' region, which occludes the active site of the protein in the crystal. The expansion of characterized members of the esterase family and demonstration of activity over a wide range of temperatures could be of use in biotechnological applications such as the pharmaceutical, detergent, bioremediation and dairy industries. |
| Type Of Material | Database/Collection of data |
| Year Produced | 2016 |
| Provided To Others? | Yes |