Valorization of biomass-based feedstocks like ethanol and furfural is paramount to a circular bioeconomy. Ethanol can be oxidized to acetaldehyde and furfural can be reduced to furfuryl alcohol, both of which are more valuable than their corresponding feedstocks. Conventional metal-based catalysts, which are used for these redox transformations require high temperatures and pressures, optionally organic solvents, and metal toxicity. Redox enzymes like yeast alcohol dehydrogenase (YADH) can catalyze substrate-coupled redox conversions at approximately 100% selectivity at high reaction rates in an aqueous medium. However, the thermodynamic and kinetic stability of the enzymes is challenged at high substrate concentrations. Additionally, using soluble enzymes limits commercial applications due to cost concerns from the loss of enzymes. In this study, YADH is immobilized on a commercial ion exchange resin with primary amine moiety via covalent bonding using glutaraldehyde as a linker. The presence of enzyme was confirmed with FTIR and enzyme loading on the resin was calculated with Bradford assay. Coupled redox transformation of ethanol and furfural to acetaldehyde and furfuryl alcohol could be catalyzed by the immobilized enzyme (YADH@GA/PA110) with reusability as demonstrated by repeated batch reactions. UV-vis spectroscopic biochemical assays of YADH@GA/PA110 are underway to assess the potential for reduced inhibition and enhanced kinetic stability of the enzyme upon immobilization.

Synthesis and characterization of immobilized yeast alcohol dehydrogenase for biomass-based feedstock valorization

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