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Six-membered cyclic carbonates from trimethylolpropane : Lipase-mediated synthesis in a flow reactor and in silico evaluation of the reaction

Bornadel, Amin LU ; Ismail, Mohamed LU orcid ; Sayed, Mahmoud LU ; Hatti-Kaul, Rajni LU and Pyo, Sang Hyun LU (2017) In Biotechnology Progress 33(2). p.375-382
Abstract

Six-membered cyclic carbonates with hydroxyl and methoxycarbonyloxy functional groups were prepared by transesterification of trimethylolpropane (TMP) with dimethylcarbonate (DMC) by solvent-free lipase-mediated flow reaction followed by thermal cyclization. The flow reaction efficiency was evaluated using different configurations of reactor consisting of packed beds of Novozym®435 (immobilized Candida antarctica lipase B—CalB—a.k.a. N435) and molecular sieves, flowrate, and biocatalyst loads. The mixed column of the biocatalyst and molecular sieves, allowing rapid and efficient removal of the by-product—methanol—was the most efficient setup. Higher conversion (81.6%) in the flow reaction compared to batch process (72%) was obtained... (More)

Six-membered cyclic carbonates with hydroxyl and methoxycarbonyloxy functional groups were prepared by transesterification of trimethylolpropane (TMP) with dimethylcarbonate (DMC) by solvent-free lipase-mediated flow reaction followed by thermal cyclization. The flow reaction efficiency was evaluated using different configurations of reactor consisting of packed beds of Novozym®435 (immobilized Candida antarctica lipase B—CalB—a.k.a. N435) and molecular sieves, flowrate, and biocatalyst loads. The mixed column of the biocatalyst and molecular sieves, allowing rapid and efficient removal of the by-product—methanol—was the most efficient setup. Higher conversion (81.6%) in the flow reaction compared to batch process (72%) was obtained using same amount of N435 (20% (w/w) N435:TMP) at 12 h, and the undesirable dimer and oligomer formation were suppressed. Moreover, the product was recovered easily without extra separation steps, and the biocatalyst and the molecular sieves remained intact for subsequent regeneration and recycling. The reaction of CalB with DMC and the primary transesterification product, monocarbonated TMP, respectively, as acyl donors was evaluated by in silico modeling and empirically to determine the role of the enzyme in the formation of cyclic carbonates and other side products. DMC was shown to be the preferred acyl donor, suggesting that TMP and its carbonated derivatives serve only as acyl acceptors in the lipase-catalyzed reaction. Subsequent cyclization to cyclic carbonate is catalyzed at increased temperature and not by the enzyme.

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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Candida antarctica lipase B (CalB, flow reaction, in silico modeling, Novozym®435), transesterification, trimethylopropane cyclic carbonate
in
Biotechnology Progress
volume
33
issue
2
pages
8 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:85006141147
  • pmid:27863151
ISSN
8756-7938
DOI
10.1002/btpr.2406
language
English
LU publication?
yes
id
ca87b1e1-cb6c-400f-a64d-42a3e0c43954
date added to LUP
2019-05-29 16:16:50
date last changed
2024-05-29 12:56:50
@article{ca87b1e1-cb6c-400f-a64d-42a3e0c43954,
  abstract     = {{<p>Six-membered cyclic carbonates with hydroxyl and methoxycarbonyloxy functional groups were prepared by transesterification of trimethylolpropane (TMP) with dimethylcarbonate (DMC) by solvent-free lipase-mediated flow reaction followed by thermal cyclization. The flow reaction efficiency was evaluated using different configurations of reactor consisting of packed beds of Novozym®435 (immobilized Candida antarctica lipase B—CalB—a.k.a. N435) and molecular sieves, flowrate, and biocatalyst loads. The mixed column of the biocatalyst and molecular sieves, allowing rapid and efficient removal of the by-product—methanol—was the most efficient setup. Higher conversion (81.6%) in the flow reaction compared to batch process (72%) was obtained using same amount of N435 (20% (w/w) N435:TMP) at 12 h, and the undesirable dimer and oligomer formation were suppressed. Moreover, the product was recovered easily without extra separation steps, and the biocatalyst and the molecular sieves remained intact for subsequent regeneration and recycling. The reaction of CalB with DMC and the primary transesterification product, monocarbonated TMP, respectively, as acyl donors was evaluated by in silico modeling and empirically to determine the role of the enzyme in the formation of cyclic carbonates and other side products. DMC was shown to be the preferred acyl donor, suggesting that TMP and its carbonated derivatives serve only as acyl acceptors in the lipase-catalyzed reaction. Subsequent cyclization to cyclic carbonate is catalyzed at increased temperature and not by the enzyme.</p>}},
  author       = {{Bornadel, Amin and Ismail, Mohamed and Sayed, Mahmoud and Hatti-Kaul, Rajni and Pyo, Sang Hyun}},
  issn         = {{8756-7938}},
  keywords     = {{Candida antarctica lipase B (CalB; flow reaction; in silico modeling; Novozym®435); transesterification; trimethylopropane cyclic carbonate}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{375--382}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biotechnology Progress}},
  title        = {{Six-membered cyclic carbonates from trimethylolpropane : Lipase-mediated synthesis in a flow reactor and in silico evaluation of the reaction}},
  url          = {{http://dx.doi.org/10.1002/btpr.2406}},
  doi          = {{10.1002/btpr.2406}},
  volume       = {{33}},
  year         = {{2017}},
}