Development of biocatalytic membrane contactor using RuBisCO as nature-inspired alternative pathway for CO2 capture and conversion

Cocon, Kamyll Dawn;Luis Alconero, Patricia
(2023) 13th International Symposium on “Scientific basis for the preparation of heterogeneous catalysts” - PREPA13 — Location: Louvain-la-Neuve (9.July.2023)

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Abstract
A biocatalytic membrane for CO2 capture and its conversion into organic compound was synthesized using Nature’s most abundant enzyme, Ribulose-1,5-Biphosphate Carboxylase/Oxygenase (RuBisCO), as a benign biocatalyst. RuBisCO was covalently immobilized on commercial flat-sheet porous polymeric membranes to improve its stability. Dopamine and polyethyleneimine were used to modify the membrane surfaces for improved enzyme compatibility, while glutaraldehyde was used as the crosslinker for immobilization. Results showed that the use of polyvinylidene fluoride (PVDF) led to higher surface amino density and higher enzyme retention compared to polypropylene (PP). However, increasing the coating duration did not necessarily led to increased enzyme retention despite the increase in surface amino density, which could be attributed to stearic hindrance. Optimization of RuBisCO activity as a function of different immobilization parameters such as coating duration, glutaraldehyde concentration, enzyme concentration, pH, incubation temperature, and enzyme immobilization duration will be made. Finally, the stability, reusability, CO2 capture and conversion performance of the optimized membrane will be evaluated. With this study, preliminary steps are taken in exploring the potential of biocatalytic membrane contactors for CO2 capture and conversion into organic compounds.
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Citations

Cocon, K. D., & Luis Alconero, P. (2023). Development of biocatalytic membrane contactor using RuBisCO as nature-inspired alternative pathway for CO2 capture and conversion. 13th International Symposium on “Scientific basis for the preparation of heterogeneous catalysts” - PREPA13, Louvain-la-Neuve. https://hdl.handle.net/2078.5/269315