Evaluation of a dye-decolorizing peroxidase from Comamonas serinivorans for lignin valorization potentials
Copyright © 2023 Elsevier B.V. All rights reserved..
Although dye-decolourising peroxidases (DyPs) are well-known for lignin degradation, a comprehensive understanding of their mechanism remains unclear. Therefore, studying the mechanism of lignin degradation by DyPs is necessary for industrial applications and enzyme engineering. In this study, a dye-decolourising peroxidase (CsDyP) gene from C. serinivorans was heterologously expressed and studied for its lignin degradation potential. Molecular docking analysis predicted the binding of 2, 2-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), veratryl alcohol (VA), 2, 6-dimethylphenol (2, 6- DMP), guaiacol (GUA), and lignin to the substrate-binding pocket of CsDyP. Evaluation of the enzymatic properties showed that CsDyP requires pH 4.0 and 30 °C for optimal activity and has a high affinity for ABTS. In addition, CsDyP is stable over a wide range of temperatures and pH and can tolerate 5.0 mM organic solvents. Low NaCl concentrations promoted CsDyP activity. Further, CsDyP significantly reduced the chemical oxygen demand decolourised alkali lignin (AL) and milled wood lignin (MWL). CsDyP targets the β-O-4, CO, and CC bonds linking lignin's G, S, and H units to depolymerize and produce aromatic compounds. Overall, this study delivers valuable insights into the lignin degradation mechanism of CsDyP, which can benefit its industrial applications and lignin valorization.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2023 |
|---|---|
| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:253 |
|---|---|
| Enthalten in: |
International journal of biological macromolecules - 253(2023), Pt 4 vom: 31. Dez., Seite 127117 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Sethupathy, Sivasamy [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 29.11.2023 Date Revised 29.11.2023 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1016/j.ijbiomac.2023.127117 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM362709238 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM362709238 | ||
| 003 | DE-627 | ||
| 005 | 20231226091810.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231226s2023 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.ijbiomac.2023.127117 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n1208.xml |
| 035 | |a (DE-627)NLM362709238 | ||
| 035 | |a (NLM)37774822 | ||
| 035 | |a (PII)S0141-8130(23)04014-X | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Sethupathy, Sivasamy |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Evaluation of a dye-decolorizing peroxidase from Comamonas serinivorans for lignin valorization potentials |
| 264 | 1 | |c 2023 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 29.11.2023 | ||
| 500 | |a Date Revised 29.11.2023 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2023 Elsevier B.V. All rights reserved. | ||
| 520 | |a Although dye-decolourising peroxidases (DyPs) are well-known for lignin degradation, a comprehensive understanding of their mechanism remains unclear. Therefore, studying the mechanism of lignin degradation by DyPs is necessary for industrial applications and enzyme engineering. In this study, a dye-decolourising peroxidase (CsDyP) gene from C. serinivorans was heterologously expressed and studied for its lignin degradation potential. Molecular docking analysis predicted the binding of 2, 2-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), veratryl alcohol (VA), 2, 6-dimethylphenol (2, 6- DMP), guaiacol (GUA), and lignin to the substrate-binding pocket of CsDyP. Evaluation of the enzymatic properties showed that CsDyP requires pH 4.0 and 30 °C for optimal activity and has a high affinity for ABTS. In addition, CsDyP is stable over a wide range of temperatures and pH and can tolerate 5.0 mM organic solvents. Low NaCl concentrations promoted CsDyP activity. Further, CsDyP significantly reduced the chemical oxygen demand decolourised alkali lignin (AL) and milled wood lignin (MWL). CsDyP targets the β-O-4, CO, and CC bonds linking lignin's G, S, and H units to depolymerize and produce aromatic compounds. Overall, this study delivers valuable insights into the lignin degradation mechanism of CsDyP, which can benefit its industrial applications and lignin valorization | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Alkali lignin | |
| 650 | 4 | |a Comamonas serinivorans | |
| 650 | 4 | |a Dye-decolorizing peroxidases | |
| 650 | 4 | |a Heterologous expression | |
| 650 | 4 | |a Lignin depolymerization | |
| 650 | 4 | |a Milled wood lignin | |
| 650 | 7 | |a Peroxidase |2 NLM | |
| 650 | 7 | |a EC 1.11.1.7 |2 NLM | |
| 650 | 7 | |a Lignin |2 NLM | |
| 650 | 7 | |a 9005-53-2 |2 NLM | |
| 650 | 7 | |a 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid |2 NLM | |
| 650 | 7 | |a 28752-68-3 |2 NLM | |
| 650 | 7 | |a Peroxidases |2 NLM | |
| 650 | 7 | |a EC 1.11.1.- |2 NLM | |
| 650 | 7 | |a Coloring Agents |2 NLM | |
| 700 | 1 | |a Xie, Rongrong |e verfasserin |4 aut | |
| 700 | 1 | |a Liang, Nian |e verfasserin |4 aut | |
| 700 | 1 | |a Shafreen, Raja Mohamed Beema |e verfasserin |4 aut | |
| 700 | 1 | |a Ali, Mohamed Yassin |e verfasserin |4 aut | |
| 700 | 1 | |a Zhuang, Zhipeng |e verfasserin |4 aut | |
| 700 | 1 | |a Zhe, Liang |e verfasserin |4 aut | |
| 700 | 1 | |a Zahoor |e verfasserin |4 aut | |
| 700 | 1 | |a Yong, Yang-Chun |e verfasserin |4 aut | |
| 700 | 1 | |a Zhu, Daochen |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t International journal of biological macromolecules |d 1992 |g 253(2023), Pt 4 vom: 31. Dez., Seite 127117 |w (DE-627)NLM012627356 |x 1879-0003 |7 nnns |
| 773 | 1 | 8 | |g volume:253 |g year:2023 |g number:Pt 4 |g day:31 |g month:12 |g pages:127117 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1016/j.ijbiomac.2023.127117 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 253 |j 2023 |e Pt 4 |b 31 |c 12 |h 127117 | ||