| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
Identification and Characterization of Carboxyl Esterases of Gill Chamber-Associated Microbiota in the Deep-Sea Shrimp Rimicaris exoculata by Using Functional Metagenomics
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| Autores: |
Alcaide, Maria
Tchigvintsev, Anatoli
Martinez-martinez, Monica
Popovic, Ana
Reva, Oleg N.
Lafraya, Alvaro
Bargiela, Rafael
Nechitaylo, Taras Y.
Matesanz, Ruth
Cambon-bonavita, Marie-anne
Jebbar, Mohamed
Yakimov, Michail M.
Savchenko, Alexei
Golyshina, Olga V.
Yakunin, Alexander F.
Golyshin, Peter N.
Ferrer, Manuel
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| Data: |
2015-03
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| Ano: |
2015
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| Resumo: |
The 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 degrees 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 degrees 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.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
http://archimer.ifremer.fr/doc/00256/36721/36438.pdf
http://archimer.ifremer.fr/doc/00256/36721/36439.pdf
DOI:10.1128/AEM.03387-14
http://archimer.ifremer.fr/doc/00256/36721/
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| Editor: |
Amer Soc Microbiology
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| Relação: |
info:eu-repo/grantAgreement/EC/FP7/226977/EU//MAMBA
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| Formato: |
application/pdf
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| Fonte: |
Applied And Environmental Microbiology (0099-2240) (Amer Soc Microbiology), 2015-03 , Vol. 81 , N. 6 , P. 2125-2136
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| Direitos: |
2015, American Society for Microbiology. All Rights Reserved.
info:eu-repo/semantics/openAccess
restricted use
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