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

Mohammed Alotaibi; Jinesh C. Manayil; Gillian M. Greenway; Stephen J. Haswell; Stephen M. Kelly; Adam F. Lee; Karen Wilson; Georgios Kyriakou

doi:10.1039/C7RE00162B

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

Mohammed Alotaibi
, Jinesh C. Manayil
, Gillian M. Greenway
, Stephen J. Haswell
, Stephen M. Kelly
, Adam F. Lee
, Karen Wilson
, Georgios Kyriakou

European Bioenergy Research Institute (EBRI)
School of Applied Science
Royal Melbourne Institute of Technology
Melbourne Health
Engineers Australia
University of Hull
UK

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

89 Downloads (Pure)

Abstract

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

Original language	English
Pages (from-to)	68-74
Journal	Reaction Chemistry & Engineering
Volume	3
Early online date	18 Dec 2017
DOIs	https://doi.org/10.1039/C7RE00162B
Publication status	Published - 2018

Bibliographical note

© Royal Society of Chemistry, 2017. Lipase immobilised on silica monoliths as continuous-flow microreactors for triglyceride transesterification
Alotaibi, M., Manayil, J. C., Greenway, G. M., Haswell, S. J., Kelly, S. M., Lee, A. F., Wilson, K. & Kyriakou, G. 18 Dec 2017 In : Reaction Chemistry & Engineering. http://doi.org/10.1039/C7RE00162B

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10.1039/C7RE00162B

Lipase immobilised on silica monoliths as continuous-flow microreactors for triglyceride transesterification
© Royal Society of Chemistry, 2017. Lipase immobilised on silica monoliths as continuous-flow microreactors for triglyceride transesterification Alotaibi, M., Manayil, J. C., Greenway, G. M., Haswell, S. J., Kelly, S. M., Lee, A. F., Wilson, K. & Kyriakou, G. 18 Dec 2017 In : Reaction Chemistry & Engineering. http://doi.org/10.1039/C7RE00162B
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title = "Lipase immobilised on silica monoliths as continuous-flow microreactors for triglyceride transesterification",

abstract = "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",

author = "Mohammed Alotaibi and Manayil, \{Jinesh C.\} and Greenway, \{Gillian M.\} and Haswell, \{Stephen J.\} and Kelly, \{Stephen M.\} and Lee, \{Adam F.\} and Karen Wilson and Georgios Kyriakou",

note = "{\textcopyright} Royal Society of Chemistry, 2017. Lipase immobilised on silica monoliths as continuous-flow microreactors for triglyceride transesterification Alotaibi, M., Manayil, J. C., Greenway, G. M., Haswell, S. J., Kelly, S. M., Lee, A. F., Wilson, K. \& Kyriakou, G. 18 Dec 2017 In : Reaction Chemistry \& Engineering. http://doi.org/10.1039/C7RE00162B",

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doi = "10.1039/C7RE00162B",

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AU - Alotaibi, Mohammed

AU - Manayil, Jinesh C.

AU - Greenway, Gillian M.

AU - Haswell, Stephen J.

AU - Kelly, Stephen M.

AU - Lee, Adam F.

AU - Wilson, Karen

AU - Kyriakou, Georgios

N1 - © Royal Society of Chemistry, 2017. Lipase immobilised on silica monoliths as continuous-flow microreactors for triglyceride transesterification Alotaibi, M., Manayil, J. C., Greenway, G. M., Haswell, S. J., Kelly, S. M., Lee, A. F., Wilson, K. & Kyriakou, G. 18 Dec 2017 In : Reaction Chemistry & Engineering. http://doi.org/10.1039/C7RE00162B

PY - 2018

Y1 - 2018

N2 - 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

AB - 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

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EP - 74

JO - Reaction Chemistry & Engineering

JF - Reaction Chemistry & Engineering

ER -

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

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