Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp

Verfasser / Beitragende:
[Luka Ausec, Miha Črnigoj, Marko Šnajder, Nataša Ulrih, Ines Mandic-Mulec]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/23(2015-12-01), 9987-9999
Format:
Artikel (online)
ID: 605504660
LEADER caa a22 4500
001 605504660
003 CHVBK
005 20210128100617.0
007 cr unu---uuuuu
008 210128e20151201xx s 000 0 eng
024 7 0 |a 10.1007/s00253-015-6843-3  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-015-6843-3 
245 0 0 |a Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp  |h [Elektronische Daten]  |c [Luka Ausec, Miha Črnigoj, Marko Šnajder, Nataša Ulrih, Ines Mandic-Mulec] 
520 3 |a Laccases are oxidoreductases mostly studied in fungi, while bacterial laccases remain poorly studied despite their high genetic diversity and potential for biotechnological application. Our previous bioinformatic analysis identified alkaliphilic bacterial strains Thioalkalivibrio sp. as potential sources of robust bacterial laccases that would be stable at high pH. In the present work, a gene for a laccase-like enzyme from Thioalkalivibrio sp. ALRh was cloned and expressed as a 6× His-tagged protein in Escherichia coli. The purified enzyme was a pH-tolerant laccase stable in the pH range between 2.1 and 9.9 at 20°C as shown by intrinsic fluorescence emission spectrometry. It had optimal activities at pH5.0 and pH9.5 with the laccase substrates 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,6-dimethoxyphenol, respectively. In addition, it could oxidize several other monophenolic compounds and potassium hexacyanoferrate(II) but not tyrosine. It showed highest activity at 50°C, making it suitable for prolonged incubations at this temperature. The present study shows that Thioalkalivibrio sp. encodes an active, alkaliphilic, and thermo-tolerant laccase and contributes to our understanding of the versatility of bacterial laccase-like multicopper oxidases in general. 
540 |a Springer-Verlag Berlin Heidelberg, 2015 
690 7 |a Laccases  |2 nationallicence 
690 7 |a Laccase-like multicopper oxidases (LMCO)  |2 nationallicence 
690 7 |a Bacterial laccases  |2 nationallicence 
690 7 |a Enzyme characterization  |2 nationallicence 
690 7 |a Thioalkalivibrio  |2 nationallicence 
700 1 |a Ausec  |D Luka  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
700 1 |a Črnigoj  |D Miha  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
700 1 |a Šnajder  |D Marko  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
700 1 |a Ulrih  |D Nataša  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
700 1 |a Mandic-Mulec  |D Ines  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/23(2015-12-01), 9987-9999  |x 0175-7598  |q 99:23<9987  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-015-6843-3  |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/s00253-015-6843-3  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Ausec  |D Luka  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Črnigoj  |D Miha  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Šnajder  |D Marko  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Ulrih  |D Nataša  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Mandic-Mulec  |D Ines  |u Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/23(2015-12-01), 9987-9999  |x 0175-7598  |q 99:23<9987  |1 2015  |2 99  |o 253