Biological conversion of methane to methanol through genetic reassembly of native catalytic domains
- Authors
- Kim, Hyun Jin; Huh, June; Kwon, Young Wan; Park, Donghyun; Yu, Yeonhwa; Jang, Young Eun; Lee, Bo-Ram; Jo, Eunji; Lee, Eun Jung; Heo, Yunseok; Lee, Weontae; Lee, Jeewon
- Issue Date
- 4월-2019
- Publisher
- NATURE PUBLISHING GROUP
- Citation
- NATURE CATALYSIS, v.2, no.4, pp.342 - 353
- Indexed
- SCIE
SCOPUS
- Journal Title
- NATURE CATALYSIS
- Volume
- 2
- Number
- 4
- Start Page
- 342
- End Page
- 353
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/66471
- DOI
- 10.1038/s41929-019-0255-1
- ISSN
- 2520-1158
- 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.
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- Appears in
Collections - College of Engineering > Department of Chemical and Biological Engineering > 1. Journal Articles
- Graduate School > KU-KIST Graduate School of Converging Science and Technology > 1. Journal Articles
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