Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase and its application

Abstract

Inducible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910 catalyzes the decarboxylation of pyrrole-2-carboxylate to stoichiometric amounts of pyrrole and CO2. A unique feature of the homodimeric enzyme is its requirement for an organic acid such as acetate, propionate, butyrate or pimelate. A catalytic mechanism including a cofactor function of the organic acid was proposed. Due to an equilibrium constant of 0.3–0.4 M, the enzyme also catalyzes the reverse carboxylation of pyrrole after the addition of bicarbonate. For the synthesis of pyrrole-2-carboxylate, the reverse reaction was optimized and the equilibrium shifted towards the carboxylate. The product yield was 230 mM (25.5 g/l) pyrrole-2-carboxylate from 300 mM pyrrole in a batch reaction and 325 mM (36.1 g/l) from 400 mM pyrrole in a fed batch reaction, using both whole cells and the purified enzyme in a pH 8.0 reaction mixture with bicarbonate saturation of 1.9 M.