FN Archimer Export Format PT J TI Identification and Characterization of Carboxyl Esterases of Gill Chamber-Associated Microbiota in the Deep-Sea Shrimp Rimicaris exoculata by Using Functional Metagenomics BT AF 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 AS 1:1;2:2;3:1;4:2;5:3;6:1;7:1;8:4;9:5;10:6;11:7;12:8;13:2;14:9;15:2;16:9;17:1; FF 1:;2:;3:;4:;5:;6:;7:;8:;9:;10:PDG-REM-EEP-LMEE;11:;12:;13:;14:;15:;16:;17:; C1 CSIC, Inst Catalysis, Madrid, Spain. Univ Toronto, Dept Chem Engn & Appl Chem, Toronto, ON, Canada. Univ Pretoria, Dept Biochem, ZA-0002 Pretoria, South Africa. Max Planck Inst Chem Ecol, Insect Symbiosis Res Grp, Jena, Germany. CSIC, Ctr Invest Biol, Madrid, Spain. Ifremer CNRS UBO, Lab Microbiol Environm Extremes, REM DEEP LM2E, Ctr Brest,UMR 6197, Plouzane, France. Univ Bretagne Occidentale, Lab Microbiol Environm Extremes, CNRS Ifremer UBO, UMR 6197, Plouzane, France. CNR, Inst Coastal Marine Environm, Messina, Italy. Bangor Univ, Sch Biol Sci, Bangor, Gwynedd, Wales. C2 CSIC, SPAIN UNIV TORONTO, CANADA UNIV PRETORIA, SOUTH AFRICA MAX PLANCK INST CHEM ECOL, GERMANY CSIC, SPAIN IFREMER, FRANCE UBO, FRANCE IAMC CNR, ITALY UNIV BANGOR, UK SI BREST SE PDG-REM-EEP-LMEE UM BEEP-LM2E IN WOS Ifremer jusqu'en 2018 copubli-france copubli-europe copubli-univ-france copubli-int-hors-europe copubli-sud IF 3.823 TC 29 UR https://archimer.ifremer.fr/doc/00256/36721/36438.pdf https://archimer.ifremer.fr/doc/00256/36721/36439.pdf LA English DT Article AB 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. PY 2015 PD MAR SO Applied And Environmental Microbiology SN 0099-2240 PU Amer Soc Microbiology VL 81 IS 6 UT 000350554800028 BP 2125 EP 2136 DI 10.1128/AEM.03387-14 ID 36721 ER EF