Characterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewater
Abstract Background 17β-estradiol (E2) residues exhibit harmful effects both for human and animals and have got global attention of the scientific community. Microbial enzymes are considered as one of the effective strategies having great potential for removal E2 residues from the environment. Howev...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
BMC
2023-06-01
|
| Series: | Microbial Cell Factories |
| Subjects: | |
| Online Access: | https://doi.org/10.1186/s12934-023-02119-w |
| _version_ | 1797789472806404096 |
|---|---|
| author | Peng Hao Hanyu Pan Zongshuo Lv Jingyi Zhang Lixia Wang Yanbin Zhu Wangdui Basang Yunhang Gao |
| author_facet | Peng Hao Hanyu Pan Zongshuo Lv Jingyi Zhang Lixia Wang Yanbin Zhu Wangdui Basang Yunhang Gao |
| author_sort | Peng Hao |
| collection | DOAJ |
| description | Abstract Background 17β-estradiol (E2) residues exhibit harmful effects both for human and animals and have got global attention of the scientific community. Microbial enzymes are considered as one of the effective strategies having great potential for removal E2 residues from the environment. However, limited literature is available on the removal of E2 from wastewater using short-chain dehydrogenase. Results In this study, 17β-estradiol degrading enzyme (17β-HSD-0095) was expressed and purified from Microbacterium sp. MZT7. The optimal pH and temperature for reaction was 7 and 40 °C, respectively. Molecular docking studies have shown that the ARG215 residue form a hydrogen bond with oxygen atom of the substrate E2. Likewise, the point mutation results have revealed that the ARG215 residue play an important role in the E2 degradation by 17β-HSD-0095. In addition, 17β-HSD-0095 could remediate E2 contamination in synthetic livestock wastewater. Conclusions These findings offer some fresh perspectives on the molecular process of E2 degradation and the creation of enzyme preparations that can degrade E2. Graphical Abstract |
| first_indexed | 2024-03-13T01:51:09Z |
| format | Article |
| id | doaj.art-0c1ecf4d15e54c20a34820e37fbadced |
| institution | Directory Open Access Journal |
| issn | 1475-2859 |
| language | English |
| last_indexed | 2024-03-13T01:51:09Z |
| publishDate | 2023-06-01 |
| publisher | BMC |
| record_format | Article |
| series | Microbial Cell Factories |
| spelling | doaj.art-0c1ecf4d15e54c20a34820e37fbadced2023-07-02T11:30:24ZengBMCMicrobial Cell Factories1475-28592023-06-0122111210.1186/s12934-023-02119-wCharacterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewaterPeng Hao0Hanyu Pan1Zongshuo Lv2Jingyi Zhang3Lixia Wang4Yanbin Zhu5Wangdui Basang6Yunhang Gao7College of Veterinary Medicine, Jilin Agricultural UniversityCollege of Veterinary Medicine, Jilin Agricultural UniversityCollege of Veterinary Medicine, Jilin Agricultural UniversityCollege of Veterinary Medicine, Jilin Agricultural UniversityNortheast Institute of Geography and Agroecology, Chinese Academy of SciencesInstitute of Animal Husbandry and Veterinary Medicine, Tibet Academy of Agriculture and Animal Husbandry ScienceInstitute of Animal Husbandry and Veterinary Medicine, Tibet Academy of Agriculture and Animal Husbandry ScienceCollege of Veterinary Medicine, Jilin Agricultural UniversityAbstract Background 17β-estradiol (E2) residues exhibit harmful effects both for human and animals and have got global attention of the scientific community. Microbial enzymes are considered as one of the effective strategies having great potential for removal E2 residues from the environment. However, limited literature is available on the removal of E2 from wastewater using short-chain dehydrogenase. Results In this study, 17β-estradiol degrading enzyme (17β-HSD-0095) was expressed and purified from Microbacterium sp. MZT7. The optimal pH and temperature for reaction was 7 and 40 °C, respectively. Molecular docking studies have shown that the ARG215 residue form a hydrogen bond with oxygen atom of the substrate E2. Likewise, the point mutation results have revealed that the ARG215 residue play an important role in the E2 degradation by 17β-HSD-0095. In addition, 17β-HSD-0095 could remediate E2 contamination in synthetic livestock wastewater. Conclusions These findings offer some fresh perspectives on the molecular process of E2 degradation and the creation of enzyme preparations that can degrade E2. Graphical Abstracthttps://doi.org/10.1186/s12934-023-02119-w17β-estradiolEnzymeRemediationWastewaterMicrobacterium sp. MZT7 |
| spellingShingle | Peng Hao Hanyu Pan Zongshuo Lv Jingyi Zhang Lixia Wang Yanbin Zhu Wangdui Basang Yunhang Gao Characterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewater Microbial Cell Factories 17β-estradiol Enzyme Remediation Wastewater Microbacterium sp. MZT7 |
| title | Characterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewater |
| title_full | Characterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewater |
| title_fullStr | Characterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewater |
| title_full_unstemmed | Characterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewater |
| title_short | Characterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewater |
| title_sort | characterization of 17β estradiol degrading enzyme from microbacterium sp mzt7 and its function on e2 biodegradation in wastewater |
| topic | 17β-estradiol Enzyme Remediation Wastewater Microbacterium sp. MZT7 |
| url | https://doi.org/10.1186/s12934-023-02119-w |
| work_keys_str_mv | AT penghao characterizationof17bestradioldegradingenzymefrommicrobacteriumspmzt7anditsfunctionone2biodegradationinwastewater AT hanyupan characterizationof17bestradioldegradingenzymefrommicrobacteriumspmzt7anditsfunctionone2biodegradationinwastewater AT zongshuolv characterizationof17bestradioldegradingenzymefrommicrobacteriumspmzt7anditsfunctionone2biodegradationinwastewater AT jingyizhang characterizationof17bestradioldegradingenzymefrommicrobacteriumspmzt7anditsfunctionone2biodegradationinwastewater AT lixiawang characterizationof17bestradioldegradingenzymefrommicrobacteriumspmzt7anditsfunctionone2biodegradationinwastewater AT yanbinzhu characterizationof17bestradioldegradingenzymefrommicrobacteriumspmzt7anditsfunctionone2biodegradationinwastewater AT wangduibasang characterizationof17bestradioldegradingenzymefrommicrobacteriumspmzt7anditsfunctionone2biodegradationinwastewater AT yunhanggao characterizationof17bestradioldegradingenzymefrommicrobacteriumspmzt7anditsfunctionone2biodegradationinwastewater |