Unknown

Dataset Information

0

Light-Driven Catalytic Upgrading of Butanol in a Biohybrid Photoelectrochemical System.


ABSTRACT: This paper reports the design and preparation of a biohybrid photoelectrochemical cell (PEC) that can drive the tandem enzymatic oxidation and aldol condensation of n-butanol (BuOH) to C8 2-ethylhexenal (2-EH). In this work, BuOH was first oxidized to n-butyraldehyde (BA) by the alcohol oxidase enzyme (AOx), concurrently generating hydrogen peroxide (H2O2). To preserve enzyme activity and increase kinetics nearly 2-fold, the H2O2 was removed by oxidation at a bismuth vanadate (BiVO4) photoanode. Organocatalyzed aldol condensation of C4 BA to C8 2-EH improved the overall BuOH conversion to 6.2 ± 0.1% in a biased PEC after 16 h. A purely light-driven, unbiased PEC showed 3.1 ± 0.1% BuOH conversion, or ~50% of that obtained from the biased system. Replacing AOx with the enzyme alcohol dehydrogenase (ADH), which requires the diffusional nicotinamide adenine dinucleotide cofactor (NAD+/NADH), resulted in only 0.2% BuOH conversion due to NAD+ dimerization at the photoanode. Lastly, the application of more positive biases with the biohybrid AOx PEC led to measurable production of H2 at the cathode, but at the cost of lower BA and 2-EH yields due to both product overoxidation and decreased enzyme activity.

SUBMITTER: Harris AW 

PROVIDER: S-EPMC7597823 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

altmetric image

Publications

Light-Driven Catalytic Upgrading of Butanol in a Biohybrid Photoelectrochemical System.

Harris Alexander W AW   Yehezkeli Omer O   Hafenstine Glenn R GR   Goodwin Andrew P AP   Cha Jennifer N JN  

ACS sustainable chemistry & engineering 20170718 9


This paper reports the design and preparation of a biohybrid photoelectrochemical cell (PEC) that can drive the tandem enzymatic oxidation and aldol condensation of <i>n</i>-butanol (BuOH) to C<sub>8</sub> 2-ethylhexenal (2-EH). In this work, BuOH was first oxidized to <i>n</i>-butyraldehyde (BA) by the alcohol oxidase enzyme (AOx), concurrently generating hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>). To preserve enzyme activity and increase kinetics nearly 2-fold, the H<sub>2</sub>O<sub>2</su  ...[more]

Similar Datasets

| S-EPMC7597829 | biostudies-literature
| S-EPMC5821488 | biostudies-literature
| S-EPMC6966697 | biostudies-literature
| S-EPMC4844906 | biostudies-literature
| S-EPMC3779845 | biostudies-other
| S-EPMC9329374 | biostudies-literature
| S-EPMC7921008 | biostudies-literature
| S-EPMC4009402 | biostudies-literature
| S-EPMC2804367 | biostudies-literature
| S-EPMC5903125 | biostudies-literature