Biooxidation of n-butane to 1-butanol by engineered P450 monooxygenase under increased pressure
메타 데이터
바이오화학분류
바이오정밀화학
용매
화학제품
연료
화장품용 기능성소재
계면활성제⁄증점제
논문
Biooxidation of n-butane to 1-butanol by engineered P450 monooxygenase under increased pressure
학술지
Journal of biotechnology
저자명
Nebel, B.A.; Scheps, D.; Honda Malca, S.; Nestl, B.M.; Breuer, M.; Wagner, H.G.; Breitscheidel, B.; Kratz, D.; Hauer, B.
초록
In addition to the traditional 1-butanol production by hydroformylation of gaseous propene and by fermentation of biomass, the cytochrome P450-catalyzed direct terminal oxidation of n-butane into the primary alcohol 1-butanol constitutes an alternative route to provide the high demand of this basic chemical. Moreover the use of n-butane offers an unexploited ubiquitous feed stock available in large quantities. Based on protein engineering of CYP153A from Polaromonas sp. JS666 and the improvement of the native redox system, a highly ω-regioselective (>96%) fusion protein variant (CYP153A<SUB>P.sp.(G254A)</SUB>-CPR<SUB>BM3</SUB>) for the conversion of n-butane into 1-butanol was developed. Maximum yield of 3.12g/L butanol, of which 2.99g/L comprise for 1-butanol, has been obtained after 20h reaction time. Due to the poor solubility of n-butane in an aqueous system, a high pressure reaction assembly was applied to increase the conversion. After optimization a maximum product content of 4.35g/L 1-butanol from a total amount of 4.53g/L butanol catalyzed by the self-sufficient fusion monooxygenase has been obtained at 15bar pressure. In comparison to the CYP153A wild type the 1-butanol concentration was enhanced fivefold using the engineered monooxygenase whole cell system by using the high-pressure reaction assembly.