Lipase immobilised on silica monoliths as continuous-flow microreactors for triglyceride transesterification

Lipase immobilised on silica monoliths has been prepared and applied as biocatalytic continuous-flow microreactors for the transesterification of tributyrin as a model bio-oil component. Candida antarctica lipase was trapped within the pores of silica monoliths, and its successful immobilisation was...

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Bibliographic Details
Published in:Reaction Chemistry & Engineering
Main Authors: Alotaibi, Mohammed, Manayil, Jinesh C., Greenway, Gillian M., Haswell, Stephen J., Kelly, Stephen M., Lee, Adam F., Wilson, Karen, Kyriakou, Georgios
Format: Article in Journal/Newspaper
Language:English
Published: Royal Society of Chemistry 2017
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Online Access:https://hull-repository.worktribe.com/file/552168/1/Article
https://hull-repository.worktribe.com/output/552168
https://doi.org/10.1039/c7re00162b
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Summary:Lipase immobilised on silica monoliths has been prepared and applied as biocatalytic continuous-flow microreactors for the transesterification of tributyrin as a model bio-oil component. Candida antarctica lipase was trapped within the pores of silica monoliths, and its successful immobilisation was demonstrated by the hydrolysis of 4-nitrophenyl butyrate to 4-nitrophenol. Lipase immobilised on silica monoliths was active for the transesterification of tributyrin at ambient temperature, with reactivity as a function of the methanol : tributyrin ratio, flow rate, temperature, and textural properties. Monoliths with a high surface area and large meso- and macropore channels enhanced the transesterification activity through improved molecule diffusion. The optimum immobilised lipase microreactor exhibited almost quantitative ester production for >100 h at 30 °C without deactivation.