Enhanced production of n-alkanes in Escherichia coli by spatial organization of biosynthetic pathway enzymes = 생합성 효소의 공간적 구성을 통한 대장균 내 n-alkane 생산 증가

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Title
Enhanced production of n-alkanes in Escherichia coli by spatial organization of biosynthetic pathway enzymes = 생합성 효소의 공간적 구성을 통한 대장균 내 n-alkane 생산 증가
Author(s)
Z Rahman; Bong Hyun Sung; J Y Yi; L M Bui; J H Lee; S C Kim
Bibliographic Citation
Journal of Biotechnology, vol. 192, no. 20, pp. 187-191
Publication Year
2014
Abstract
Alkanes chemically mimic hydrocarbons found in petroleum, and their demand as biofuels is steadily increasing. Biologically, n-alkanes are produced from fatty acyl-ACPs by acyl-ACP reductases (AARs) and aldehyde deformylating oxygenases (ADOs). One of the major impediments in n-alkane biosynthesis is the low catalytic turnover rates of ADOs. Here, we studied n-alkane biosynthesis in Escherichia coli using a chimeric ADO-AAR fusion protein or zinc finger protein-guided ADO/AAR assembly on DNA scaffolds to control their stoichiometric ratios and spatial arrangements. Bacterial production of n-alkanes with the ADO-AAR fusion protein was increased 4.8-fold (24. mg/L) over a control strain expressing ADO and AAR separately. Optimal n-alkane biosynthesis was achieved when the ADO:AAR binding site ratio on a DNA scaffold was 3:1, yielding an 8.8-fold increase (44. mg/L) over the control strain. Our findings indicate that the spatial organization of alkane-producing enzymes is critical for efficient n-alkane biosynthesis in E. coli.
Keyword
AlkanesBiofuelChimeric expressionDNA scaffoldSynthetic biology
ISSN
0168-1656
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.jbiotec.2014.10.014
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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