Engineering globins for efficient biodegradation of malachite green: two case studies of myoglobin and neuroglobin. Issue 29 (24th June 2022)
- Record Type:
- Journal Article
- Title:
- Engineering globins for efficient biodegradation of malachite green: two case studies of myoglobin and neuroglobin. Issue 29 (24th June 2022)
- Main Title:
- Engineering globins for efficient biodegradation of malachite green: two case studies of myoglobin and neuroglobin
- Authors:
- Liu, Jiao
Xu, Jia-Kun
Yuan, Hong
Wang, Xiao-Juan
Gao, Shu-Qin
Wen, Ge-Bo
Tan, Xiang-Shi
Lin, Ying-Wu - Abstract:
- Abstract : Engineered globins such as H64D Mb and A15C/H64D Ngb were efficient in the degradation of malachite green, with activities much higher than those of some native enzymes. Abstract : Malachite green (MG)-contaminated wastewater resulting from industrialization causes a global problem because of its toxicity and widespread usage. Compared with traditional physical and chemical approaches, biodegradation provides a new route for the degradation of MG. As promising candidates for native enzymes, artificial enzymes have received tremendous attention for potential applications due to unlimited possibilities based on precise design. In this study, we rationally engineered artificial enzymes based on myoglobin (Mb) and neuroglobin (Ngb). We introduced an aspartic acid (H64D mutation) in the heme pocket of Mb. A distal histidine (F43H mutation) was further introduced into H64D Mb to obtain a double mutant of F43H/H64D Mb. Moreover, we used A15C/H64D Ngb as designed recently for comparison studies. The H64D Mb, F43H/H64D Mb, and A15C/H64D Ngb were found to catalyze MG degradation efficiently, with activities much higher than those of native enzymes, such as dye-decolorizing peroxidase and laccase (83–205-fold). The crystal structure of H64D Mb was solved and the interactions of MG and H64D Mb and A15C/H64D Ngb were investigated by using both experimental and molecular docking studies. The biodegradation products of MG were also revealed by ESI-MS analysis. Therefore, theseAbstract : Engineered globins such as H64D Mb and A15C/H64D Ngb were efficient in the degradation of malachite green, with activities much higher than those of some native enzymes. Abstract : Malachite green (MG)-contaminated wastewater resulting from industrialization causes a global problem because of its toxicity and widespread usage. Compared with traditional physical and chemical approaches, biodegradation provides a new route for the degradation of MG. As promising candidates for native enzymes, artificial enzymes have received tremendous attention for potential applications due to unlimited possibilities based on precise design. In this study, we rationally engineered artificial enzymes based on myoglobin (Mb) and neuroglobin (Ngb). We introduced an aspartic acid (H64D mutation) in the heme pocket of Mb. A distal histidine (F43H mutation) was further introduced into H64D Mb to obtain a double mutant of F43H/H64D Mb. Moreover, we used A15C/H64D Ngb as designed recently for comparison studies. The H64D Mb, F43H/H64D Mb, and A15C/H64D Ngb were found to catalyze MG degradation efficiently, with activities much higher than those of native enzymes, such as dye-decolorizing peroxidase and laccase (83–205-fold). The crystal structure of H64D Mb was solved and the interactions of MG and H64D Mb and A15C/H64D Ngb were investigated by using both experimental and molecular docking studies. The biodegradation products of MG were also revealed by ESI-MS analysis. Therefore, these artificial enzymes have potential applications in the biodegradation of MG in textile industries and fisheries. … (more)
- Is Part Of:
- RSC advances. Volume 12:Issue 29(2022)
- Journal:
- RSC advances
- Issue:
- Volume 12:Issue 29(2022)
- Issue Display:
- Volume 12, Issue 29 (2022)
- Year:
- 2022
- Volume:
- 12
- Issue:
- 29
- Issue Sort Value:
- 2022-0012-0029-0000
- Page Start:
- 18654
- Page End:
- 18660
- Publication Date:
- 2022-06-24
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d2ra02795j ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 22261.xml