Identification and Characterization of Carboxyl Esterases of Gill Chamber-Associated Microbiota in the Deep-Sea Shrimp Rimicaris exoculata by Using Functional Metagenomics

Type Article
Date 2015-03
Language English
Author(s) Alcaide Maria1, Tchigvintsev Anatoli2, Martinez-Martinez Monica1, Popovic Ana2, Reva Oleg N.3, Lafraya Alvaro1, Bargiela Rafael1, Nechitaylo Taras Y.4, Matesanz Ruth5, Cambon-Bonavita Marie-AnneORCID6, Jebbar Mohamed7, Yakimov Michail M.8, Savchenko Alexei2, Golyshina Olga V.9, Yakunin Alexander F.2, Golyshin Peter N.9, Ferrer Manuel1
Affiliation(s) 1 : CSIC, Inst Catalysis, Madrid, Spain.
2 : Univ Toronto, Dept Chem Engn & Appl Chem, Toronto, ON, Canada.
3 : Univ Pretoria, Dept Biochem, ZA-0002 Pretoria, South Africa.
4 : Max Planck Inst Chem Ecol, Insect Symbiosis Res Grp, Jena, Germany.
5 : CSIC, Ctr Invest Biol, Madrid, Spain.
6 : Ifremer CNRS UBO, Lab Microbiol Environm Extremes, REM DEEP LM2E, Ctr Brest,UMR 6197, Plouzane, France.
7 : Univ Bretagne Occidentale, Lab Microbiol Environm Extremes, CNRS Ifremer UBO, UMR 6197, Plouzane, France.
8 : CNR, Inst Coastal Marine Environm, Messina, Italy.
9 : Bangor Univ, Sch Biol Sci, Bangor, Gwynedd, Wales.
Source Applied And Environmental Microbiology (0099-2240) (Amer Soc Microbiology), 2015-03 , Vol. 81 , N. 6 , P. 2125-2136
DOI 10.1128/AEM.03387-14
WOS© Times Cited 30
Abstract 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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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 (2015). Identification and Characterization of Carboxyl Esterases of Gill Chamber-Associated Microbiota in the Deep-Sea Shrimp Rimicaris exoculata by Using Functional Metagenomics. Applied And Environmental Microbiology, 81(6), 2125-2136. Publisher's official version : https://doi.org/10.1128/AEM.03387-14 , Open Access version : https://archimer.ifremer.fr/doc/00256/36721/