The environment shapes microbial enzymes: five cold-active and salt-resistant carboxylesterases from marine metagenomes

Verfasser / Beitragende:
[Anatoli Tchigvintsev, Hai Tran, Ana Popovic, Filip Kovacic, Greg Brown, Robert Flick, Mahbod Hajighasemi, Olga Egorova, Joseph Somody, Dmitri Tchigvintsev, Anna Khusnutdinova, Tatyana Chernikova, Olga Golyshina, Michail Yakimov, Alexei Savchenko, Peter Golyshin, Karl-Erich Jaeger, Alexander Yakunin]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/5(2015-03-01), 2165-2178
Format:
Artikel (online)
ID: 605504431
LEADER caa a22 4500
001 605504431
003 CHVBK
005 20210128100616.0
007 cr unu---uuuuu
008 210128e20150301xx s 000 0 eng
024 7 0 |a 10.1007/s00253-014-6038-3  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-014-6038-3 
245 0 4 |a The environment shapes microbial enzymes: five cold-active and salt-resistant carboxylesterases from marine metagenomes  |h [Elektronische Daten]  |c [Anatoli Tchigvintsev, Hai Tran, Ana Popovic, Filip Kovacic, Greg Brown, Robert Flick, Mahbod Hajighasemi, Olga Egorova, Joseph Somody, Dmitri Tchigvintsev, Anna Khusnutdinova, Tatyana Chernikova, Olga Golyshina, Michail Yakimov, Alexei Savchenko, Peter Golyshin, Karl-Erich Jaeger, Alexander Yakunin] 
520 3 |a Most of the Earth's biosphere is cold and is populated by cold-adapted microorganisms. To explore the natural enzyme diversity of these environments and identify new carboxylesterases, we have screened three marine metagenome gene libraries for esterase activity. The screens identified 23 unique active clones, from which five highly active esterases were selected for biochemical characterization. The purified metagenomic esterases exhibited high activity against α-naphthyl and p-nitrophenyl esters with different chain lengths. All five esterases retained high activity at 5°C indicating that they are cold-adapted enzymes. The activity of MGS0010 increased more than two times in the presence of up to 3.5M NaCl or KCl, whereas the other four metagenomic esterases were inhibited to various degrees by these salts. The purified enzymes showed different sensitivities to inhibition by solvents and detergents, and the activities of MGS0010, MGS0105 and MGS0109 were stimulated three to five times by the addition of glycerol. Screening of purified esterases against 89 monoester substrates revealed broad substrate profiles with a preference for different esters. The metagenomic esterases also hydrolyzed several polyester substrates including polylactic acid suggesting that they can be used for polyester depolymerization. Thus, esterases from marine metagenomes are cold-adapted enzymes exhibiting broad biochemical diversity reflecting the environmental conditions where they evolved. 
540 |a Springer-Verlag Berlin Heidelberg, 2014 
690 7 |a Marine metagenome  |2 nationallicence 
690 7 |a Metagenomic library  |2 nationallicence 
690 7 |a Esterase  |2 nationallicence 
690 7 |a Cold adaptation  |2 nationallicence 
690 7 |a Salt resistance  |2 nationallicence 
690 7 |a Polyester hydrolysis  |2 nationallicence 
700 1 |a Tchigvintsev  |D Anatoli  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Tran  |D Hai  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Popovic  |D Ana  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Kovacic  |D Filip  |u Institute of Molecular Enzyme Technology, Heinrich-Heine-University Duesseldorf, Forschungszentrum Juelich, 52426, Juelich, Germany  |4 aut 
700 1 |a Brown  |D Greg  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Flick  |D Robert  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Hajighasemi  |D Mahbod  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Egorova  |D Olga  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Somody  |D Joseph  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Tchigvintsev  |D Dmitri  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Khusnutdinova  |D Anna  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Chernikova  |D Tatyana  |u School of Biological Sciences, Bangor University, LL57 2UW, Gwynedd, UK  |4 aut 
700 1 |a Golyshina  |D Olga  |u School of Biological Sciences, Bangor University, LL57 2UW, Gwynedd, UK  |4 aut 
700 1 |a Yakimov  |D Michail  |u Institute for Coastal Marine Environment, CNR, 98122, Messina, Italy  |4 aut 
700 1 |a Savchenko  |D Alexei  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
700 1 |a Golyshin  |D Peter  |u School of Biological Sciences, Bangor University, LL57 2UW, Gwynedd, UK  |4 aut 
700 1 |a Jaeger  |D Karl-Erich  |u Institute of Molecular Enzyme Technology, Heinrich-Heine-University Duesseldorf, Forschungszentrum Juelich, 52426, Juelich, Germany  |4 aut 
700 1 |a Yakunin  |D Alexander  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/5(2015-03-01), 2165-2178  |x 0175-7598  |q 99:5<2165  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-014-6038-3  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00253-014-6038-3  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Tchigvintsev  |D Anatoli  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Tran  |D Hai  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Popovic  |D Ana  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Kovacic  |D Filip  |u Institute of Molecular Enzyme Technology, Heinrich-Heine-University Duesseldorf, Forschungszentrum Juelich, 52426, Juelich, Germany  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Brown  |D Greg  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Flick  |D Robert  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Hajighasemi  |D Mahbod  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Egorova  |D Olga  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Somody  |D Joseph  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Tchigvintsev  |D Dmitri  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Khusnutdinova  |D Anna  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Chernikova  |D Tatyana  |u School of Biological Sciences, Bangor University, LL57 2UW, Gwynedd, UK  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Golyshina  |D Olga  |u School of Biological Sciences, Bangor University, LL57 2UW, Gwynedd, UK  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Yakimov  |D Michail  |u Institute for Coastal Marine Environment, CNR, 98122, Messina, Italy  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Savchenko  |D Alexei  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Golyshin  |D Peter  |u School of Biological Sciences, Bangor University, LL57 2UW, Gwynedd, UK  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Jaeger  |D Karl-Erich  |u Institute of Molecular Enzyme Technology, Heinrich-Heine-University Duesseldorf, Forschungszentrum Juelich, 52426, Juelich, Germany  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Yakunin  |D Alexander  |u Department of Chemical Engineering and Applied Chemistry, University of Toronto, M5S 3E5, Toronto, ON, Canada  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/5(2015-03-01), 2165-2178  |x 0175-7598  |q 99:5<2165  |1 2015  |2 99  |o 253