Enoate reductase from Bacillus coagulans (ERBC) is a promising biocatalyst that has been shown to reduce the carbon-carbon double bonds of cis,cis-muconic acid in vivo, generating adipic acid, an important precursor used in the synthesis nylon-6,6. Our research has shown that ERBC is capable of reducing carbon-carbon double bonds in a variety of molecules produced using the extradiol dioxygenase BphC. Since the native substrate of ERBC is unknown, studying its activity with a variety of similar substrates will be beneficial for evaluating the scope of its reactivity. Our research aims to identify promising substrates using UV-visible light spectroscopy and to characterize enzymatic products through high performance liquid chromatography (HPLC) analysis. Identification of possible substrates and subsequent engineering and enhancement of the catalytic activity of ERBC can enable the development of environmentally benign synthetic methods for the production of a variety of commodity chemicals.
