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Identification and characterization of carboxyl esterases of gill chamber-associated microbiota in the deep-sea shrimp Rimicaris exoculata using functional metagenomics

Alcaide, M. and Tchigvinstsev, A. and Martinez-Martinez, M. and Popovic, A. and Reva, O.N. and Lafraya, A. and Bargiela, R.: Nechitaylo T.Y. and Matesanz, R. and Cambon-Bonavita, M. and Jebbar, M. and Yakimov, M.M. and Savchenko, A. and Golyshina, O.V. and Yakunin, A.F. and Golyshin, P.N. and Ferrer, M. and The MAMBA Consortium., (2015) Identification and characterization of carboxyl esterases of gill chamber-associated microbiota in the deep-sea shrimp Rimicaris exoculata using functional metagenomics. Applied and Environmental Microbiology, 81 (6). pp. 2125-2136. DOI: 10.1128/AEM.03387-14

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Abstract

The shrimp Rimicaris exoculata dominates the fauna in deep-sea hydrothermal vent sites along the Mid-Atlantic Ridge (2,320 m depth). Here, we identified and biochemically characterized three carboxyl esterases from microbial communities inhabiting the R. exoculata gill, isolated by naïve screens of a gill metagenomic library. These proteins exhibit low to moderate identity to known esterase sequences (�52%) and to each other (11.9-63.7%) and appear to have originated from unknown species or from genera of Proteobacteria related to Thiothrix/Leucothrix (MGS-RG1/RG2) and to the Rhodobacteraceae group (MGS-RG3). A library of 131 esters and 31 additional esterase/lipase preparations was used to evaluate the activity profiles of these enzymes. All 3 of these enzymes had greater esterase than lipase activity and exhibited specific activities with ester substrates (�356 units mg-1) in the range of similar enzymes. MGS-RG3 was inhibited by salts and pressure and had a low optimal temperature (30°C), and its substrate profile clustered within a group of low-active and substrate-restricted marine enzymes. In contrast, MGS-RG1 and MGS-RG2 were most active at 45-50°C, were salt-activated and baro-tolerant. They also exhibited wider substrate profiles that were close to those of highly active promiscuous enzymes from a marine hydrothermal vent (MGS-RG2) and from cold brackish lake (MGS-RG1). The data presented are discussed in the context of promoting the examination of enzyme activities of taxa found in habitats that have been hitherto neglected for enzyme prospecting; the enzymes found in these taxa may reflect distinct habitat-specific adaptations and may constitute new sources of rare reaction specificities.

Item Type: Article
Subjects: Research Publications
Departments: College of Natural Sciences > School of Biological Sciences
Date Deposited: 02 Apr 2016 03:14
Last Modified: 02 Apr 2016 03:14
ISSN: 0099-2240
URI: http://e.bangor.ac.uk/id/eprint/6437
Identification Number: DOI: 10.1128/AEM.03387-14
Publisher: American Society for Microbiology
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