Boosting the acetol production in methanotrophic biocatalyst Methylomonas sp. DH-1 by the coupling activity of heteroexpressed novel protein PmoD with endogenous particulate methane monooxygenase.
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| Title: | Boosting the acetol production in methanotrophic biocatalyst Methylomonas sp. DH-1 by the coupling activity of heteroexpressed novel protein PmoD with endogenous particulate methane monooxygenase. |
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| Authors: | Chau, Tin Hoang Trung1 (AUTHOR), Nguyen, Anh Duc1 (AUTHOR), Lee, Eun Yeol1 (AUTHOR) eunylee@khu.ac.kr |
| Source: | Biotechnology for Biofuels & Bioproducts. 1/17/2022, Vol. 15 Issue 1, p1-13. 13p. |
| Subjects: | Hydroxypropanone, Enzymes, Carrier proteins, Monooxygenases, Membrane proteins, Operons |
| Abstract: | Background: Methylacidiphilum sp. IT6 has been validated its C3 substrate assimilation pathway via acetol as a key intermediate using the PmoCAB3, a homolog of the particulate methane monooxygenase (pMMO). From the transcriptomic data, the contribution of PmoD of strain IT6 in acetone oxidation was questioned. Methylomonas sp. DH-1, a type I methanotroph containing pmo operon without the existence of its pmoD, has been deployed as a biocatalyst for the gas-to-liquid bioconversion of methane and propane to methanol and acetone. Thus, Methylomonas sp. DH-1 is a suitable host for investigation. The PmoD-expressed Methylomonas sp. DH-1 can also be deployed for acetol production, a well-known intermediate for various industrial applications. Microbial production of acetol is a sustainable approach attracted attention so far. Results: In this study, bioinformatics analyses elucidated that novel protein PmoD is a C-terminal transmembrane–helix membrane with the proposed function as a transport protein. Furthermore, the whole-cell biocatalyst was constructed in Methylomonas sp. DH-1 by co-expression the PmoD of Methylacidiphilum sp. IT6 with the endogenous pMMO to enable acetone oxidation. Under optimal conditions, the maximum accumulation, and specific productivity of acetol were 18.291 mM (1.35 g/L) and 0.317 mmol/g cell/h, respectively. The results showed the first coupling activity of pMMO with a heterologous protein PmoD, validated the involvement of PmoD in acetone oxidation, and demonstrated an unprecedented production of acetol from acetone in type I methanotrophic biocatalyst. From the data achieved in batch cultivation conditions, an assimilation pathway of acetone via acetol as the key intermediate was also proposed. Conclusion: Using bioinformatics tools, the protein PmoD has been elucidated as the membrane protein with the proposed function as a transport protein. Furthermore, results from the assays of PmoD-heteroexpressed Methylomonas sp. DH-1 as a whole-cell biocatalyst validated the coupling activity of PmoD with pMMO to convert acetone to acetol, which also unlocks the potential of this recombinant biocatalyst for acetol production. The proposed acetone-assimilated pathway in the recombinant Methylomonas sp. DH-1, once validated, can extend the metabolic flexibility of Methylomonas sp. DH-1. [ABSTRACT FROM AUTHOR] |
| Copyright of Biotechnology for Biofuels & Bioproducts is the property of BioMed Central and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
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| Header | DbId: egs DbLabel: Engineering Source An: 155153289 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Boosting the acetol production in methanotrophic biocatalyst Methylomonas sp. DH-1 by the coupling activity of heteroexpressed novel protein PmoD with endogenous particulate methane monooxygenase. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Chau%2C+Tin+Hoang+Trung%22">Chau, Tin Hoang Trung</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Nguyen%2C+Anh+Duc%22">Nguyen, Anh Duc</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lee%2C+Eun+Yeol%22">Lee, Eun Yeol</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> eunylee@khu.ac.kr</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Biotechnology+for+Biofuels+%26+Bioproducts%22">Biotechnology for Biofuels & Bioproducts</searchLink>. 1/17/2022, Vol. 15 Issue 1, p1-13. 13p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Hydroxypropanone%22">Hydroxypropanone</searchLink><br /><searchLink fieldCode="DE" term="%22Enzymes%22">Enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Carrier+proteins%22">Carrier proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Monooxygenases%22">Monooxygenases</searchLink><br /><searchLink fieldCode="DE" term="%22Membrane+proteins%22">Membrane proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Operons%22">Operons</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Background: Methylacidiphilum sp. IT6 has been validated its C3 substrate assimilation pathway via acetol as a key intermediate using the PmoCAB3, a homolog of the particulate methane monooxygenase (pMMO). From the transcriptomic data, the contribution of PmoD of strain IT6 in acetone oxidation was questioned. Methylomonas sp. DH-1, a type I methanotroph containing pmo operon without the existence of its pmoD, has been deployed as a biocatalyst for the gas-to-liquid bioconversion of methane and propane to methanol and acetone. Thus, Methylomonas sp. DH-1 is a suitable host for investigation. The PmoD-expressed Methylomonas sp. DH-1 can also be deployed for acetol production, a well-known intermediate for various industrial applications. Microbial production of acetol is a sustainable approach attracted attention so far. Results: In this study, bioinformatics analyses elucidated that novel protein PmoD is a C-terminal transmembrane–helix membrane with the proposed function as a transport protein. Furthermore, the whole-cell biocatalyst was constructed in Methylomonas sp. DH-1 by co-expression the PmoD of Methylacidiphilum sp. IT6 with the endogenous pMMO to enable acetone oxidation. Under optimal conditions, the maximum accumulation, and specific productivity of acetol were 18.291 mM (1.35 g/L) and 0.317 mmol/g cell/h, respectively. The results showed the first coupling activity of pMMO with a heterologous protein PmoD, validated the involvement of PmoD in acetone oxidation, and demonstrated an unprecedented production of acetol from acetone in type I methanotrophic biocatalyst. From the data achieved in batch cultivation conditions, an assimilation pathway of acetone via acetol as the key intermediate was also proposed. Conclusion: Using bioinformatics tools, the protein PmoD has been elucidated as the membrane protein with the proposed function as a transport protein. Furthermore, results from the assays of PmoD-heteroexpressed Methylomonas sp. DH-1 as a whole-cell biocatalyst validated the coupling activity of PmoD with pMMO to convert acetone to acetol, which also unlocks the potential of this recombinant biocatalyst for acetol production. The proposed acetone-assimilated pathway in the recombinant Methylomonas sp. DH-1, once validated, can extend the metabolic flexibility of Methylomonas sp. DH-1. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Biotechnology for Biofuels & Bioproducts is the property of BioMed Central and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1186/s13068-022-02105-1 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 13 StartPage: 1 Subjects: – SubjectFull: Hydroxypropanone Type: general – SubjectFull: Enzymes Type: general – SubjectFull: Carrier proteins Type: general – SubjectFull: Monooxygenases Type: general – SubjectFull: Membrane proteins Type: general – SubjectFull: Operons Type: general Titles: – TitleFull: Boosting the acetol production in methanotrophic biocatalyst Methylomonas sp. DH-1 by the coupling activity of heteroexpressed novel protein PmoD with endogenous particulate methane monooxygenase. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Chau, Tin Hoang Trung – PersonEntity: Name: NameFull: Nguyen, Anh Duc – PersonEntity: Name: NameFull: Lee, Eun Yeol IsPartOfRelationships: – BibEntity: Dates: – D: 17 M: 01 Text: 1/17/2022 Type: published Y: 2022 Identifiers: – Type: issn-print Value: 27313654 Numbering: – Type: volume Value: 15 – Type: issue Value: 1 Titles: – TitleFull: Biotechnology for Biofuels & Bioproducts Type: main |
| ResultId | 1 |
