Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp
Gespeichert in:
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)
Online Zugang:
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| 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 | |
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| 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 | ||
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| 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 | ||