Journal
NATURE CATALYSIS
Volume 2, Issue 4, Pages 342-353Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41929-019-0255-1
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Funding
- 2015 NLRL (National Leading Research Lab.) Project [NRF (National Research Foundation Korea)-2015R1A2A1A05001861]
- Bio & Medical Technology Development Program [NRF-2017M3A9F5032628]
- NRF-Korea [NRF-2016R1A6A3A11933393]
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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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