Abstract
The study examines the role of magnetite (1–150 mg/L) at the interface of Bacillus subtilis-electrode under poised-condition (-0.2 V) for product-formation and catalytic-conduct with the relative-gene-expression encoding lactate dehydrogenase (lctE), pyruvate dehydrogenase (pdhA), acetate kinase (ackA), pyruvate carboxylase (pycA), and NADH dehydrogenase (ndh). The magnetite load of 25 mg/L showed positive influence on acidogenesis resulting in H2 production of 264.7 mol/mL and fatty acids synthesis of 3.6 g/L. Additionally, this condition showed higher succinic acid productivity (2.8 g/L) which correlates with the upregulated pycA gene and fumarate to succinate redox peak. With 10 mg/L loading, production of higher acetic acid (3.1 g/L) along with H2 (181.6 mol/mL) was depicted wherein upregulation of pdhA, ackA and ndh genes was observed. In absence of magnetite, lctE gene was upregulated which resulted higher lactate production. The findings suggest that the mutual-interactions between magnetite-active sites of specific enzymes enhances the biocatalytic activity triggering product-formation.
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