Biological conversion of methane to methanol through genetic reassembly of native catalytic domains

Hyun Jin Kim, June Huh, Young Wan Kwon, Donghyun Park, Yeonhwa Yu, Young Eun Jang, Bo Ram Lee, Eunji Jo, Eun Jung Lee, Yunseok Heo, Weontae Lee, Jeewon Lee

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Methane monooxygenase (MMO), which exists in particulate (pMMO) or soluble forms (sMMO) in methanotrophic bacteria, is an industrially promising enzyme that catalyses oxidation of low-reactive methane and other carbon feedstocks into methanol and their corresponding oxidation products. However, the simple, fast and high-yield production of functionally active MMO, which has so far been unsuccessful despite diverse approaches based on either native methanotroph culture or recombinant expression systems, remains a major challenge for its industrial applications. Here we developed pMMO-mimetic catalytic protein constructs by genetically encoding the beneficial reassembly of catalytic domains of pMMO on apoferritin as a biosynthetic scaffold. This approach resulted in high-yield synthesis of stable and soluble protein constructs in Escherichia coli, which successfully retain enzymatic activity for methanol production with a turnover number comparable to that of native pMMO.

Original languageEnglish
Pages (from-to)342-353
Number of pages12
JournalNature Catalysis
Volume2
Issue number4
DOIs
Publication statusPublished - 2019 Apr 1

ASJC Scopus subject areas

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology

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    Kim, H. J., Huh, J., Kwon, Y. W., Park, D., Yu, Y., Jang, Y. E., Lee, B. R., Jo, E., Lee, E. J., Heo, Y., Lee, W., & Lee, J. (2019). Biological conversion of methane to methanol through genetic reassembly of native catalytic domains. Nature Catalysis, 2(4), 342-353. https://doi.org/10.1038/s41929-019-0255-1