Team:UANL Mty-Mexico/Project/abstract
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<p><br><h3>Abstract</h3><br></p> | <p><br><h3>Abstract</h3><br></p> | ||
- | <p>One of the major environmental problems in northern Mexico is arsenic contamination of groundwater. Several projects have previously aimed to | + | <p>One of the major environmental problems in northern Mexico is arsenic contamination of groundwater. Several projects have previously aimed to bioremediate heavy metals and metalloids using bacteria, but without scalable potential due to the lack of an efficient cell recovery system. |
We aim to develop an easy-to-recover arsenic biosensor and chelator. Recovery strategy will consist of a new adhesion mechanism that enables bacteria to bind to silica surfaces through the expression of the L2 ribosomal protein, attached to the outer membrane protein AIDA-I. A quantifiable, highly-sensitive luciferase-based reporter system coupled to an oligomeric metallothionein is expected to increase our system’s capability of arsenic sensing and chelation.</p> | We aim to develop an easy-to-recover arsenic biosensor and chelator. Recovery strategy will consist of a new adhesion mechanism that enables bacteria to bind to silica surfaces through the expression of the L2 ribosomal protein, attached to the outer membrane protein AIDA-I. A quantifiable, highly-sensitive luciferase-based reporter system coupled to an oligomeric metallothionein is expected to increase our system’s capability of arsenic sensing and chelation.</p> | ||
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Revision as of 01:20, 27 September 2012
Abstract
One of the major environmental problems in northern Mexico is arsenic contamination of groundwater. Several projects have previously aimed to bioremediate heavy metals and metalloids using bacteria, but without scalable potential due to the lack of an efficient cell recovery system. We aim to develop an easy-to-recover arsenic biosensor and chelator. Recovery strategy will consist of a new adhesion mechanism that enables bacteria to bind to silica surfaces through the expression of the L2 ribosomal protein, attached to the outer membrane protein AIDA-I. A quantifiable, highly-sensitive luciferase-based reporter system coupled to an oligomeric metallothionein is expected to increase our system’s capability of arsenic sensing and chelation.