Data/hora: 14/06/2024 21:54:58

Provedor de dados: | 5
País: | France
Título: | Identification and Characterization of Carboxyl Esterases of Gill Chamber-Associated Microbiota in the Deep-Sea Shrimp Rimicaris exoculata by Using Functional Metagenomics
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.
Data: | 2015-03
Ano: | 2015
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 (&lt;= 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 (&lt;= 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.
Tipo: | Text
Idioma: | Inglês

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/

Editor: | Amer Soc Microbiology
Relação: | info:eu-repo/grantAgreement/EC/FP7/226977/EU//MAMBA
Formato: | application/pdf
Fonte: | Applied And Environmental Microbiology (0099-2240) (Amer Soc Microbiology), 2015-03 , Vol. 81 , N. 6 , P. 2125-2136

Fonte:

2015, American Society for Microbiology. All Rights Reserved.

info:eu-repo/semantics/openAccess

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