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 language | English |
|---|---|
| Pages (from-to) | 342-353 |
| Number of pages | 12 |
| Journal | Nature Catalysis |
| Volume | 2 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2019 Apr 1 |
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All Science Journal Classification (ASJC) codes
- Catalysis
- Bioengineering
- Biochemistry
- Process Chemistry and Technology
Cite this
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Biological conversion of methane to methanol through genetic reassembly of native catalytic domains. / 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.
In: Nature Catalysis, Vol. 2, No. 4, 01.04.2019, p. 342-353.Research output: Contribution to journal › Article
TY - JOUR
T1 - Biological conversion of methane to methanol through genetic reassembly of native catalytic domains
AU - Kim, Hyun Jin
AU - Huh, June
AU - Kwon, Young Wan
AU - Park, Donghyun
AU - Yu, Yeonhwa
AU - Jang, Young Eun
AU - Lee, Bo Ram
AU - Jo, Eunji
AU - Lee, Eun Jung
AU - Heo, Yunseok
AU - Lee, Weontae
AU - Lee, Jeewon
PY - 2019/4/1
Y1 - 2019/4/1
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=85063758112&partnerID=8YFLogxK
U2 - 10.1038/s41929-019-0255-1
DO - 10.1038/s41929-019-0255-1
M3 - Article
AN - SCOPUS:85063758112
VL - 2
SP - 342
EP - 353
JO - Nature Catalysis
JF - Nature Catalysis
SN - 2520-1158
IS - 4
ER -