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Title

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

AuthorsAlcaide, María ; Tchigvintsev, Anatoli; Martínez-Martínez, Mónica ; Popovic, Ana; Reva, Oleg; Lafraya Aguado, Álvaro ; Bargiela, Rafael ; Nechitaylo, Taras Y.; Matesanz, Ruth ; Cambon-Bonavita, M. A.; Jebbar, M.; Yakimov, Michail M.; Savchenko, Alexei; Golyshina, Olga V. ; Yakunin, Alexander F.; Golyshin, Peter N.; Ferrer, Manuel
Issue DateMar-2015
PublisherAmerican Society for Microbiology
CitationApplied and Environmental Microbiology 81(6): 2125-2136 (2015)
AbstractThe shrimp Rimicaris exoculata dominates the fauna in deep-sea hydrothermal vent sites along the Mid-Atlantic Ridge (depth, 2,320 m). Here, we identified and biochemically characterized three carboxyl esterases from microbial communities inhabiting the R. exoculata gill that were isolated by naive screens of a gill chamber metagenomic library. These proteins exhibit low to moderate identity to known esterase sequences (≤52%) and to each other (11.9 to 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 U 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-activity and substrate-restricted marine enzymes. In contrast, MGS-RG1 and MGS-RG2 were most active at 45 to 50°C and were salt activated and barotolerant. 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 a 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 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.
Publisher version (URL)https://doi.org/10.1128/AEM.03387-14
URIhttp://hdl.handle.net/10261/189732
DOI10.1128/AEM.03387-14
ISSN0099-2240
E-ISSN1098-5336
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