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Special Issue "Biocatalysis and Biotransformations in Organic Synthesis"

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A special issue of Molecules (ISSN 1420-3049).

Deadline for manuscript submissions: closed (20 September 2012)

Special Issue Editor

Guest Editor
Dr. Ioulia Smonou

Department of Chemistry, University of Crete, Campus Voutes-Heraklion, 71003 Crete, Greece
Website | E-Mail
Interests: biocatalysis-biotransformations in organic synthesis; asymmetric synthesis of bioactive compounds using biocatalytic methods; applied biocatalysis; mechanisms of organic reactions

Special Issue Information

Dear Colleagues,

The contribution of Biocatalysis and Biotransformations in Organic Synthesis (BBOS) is of increasing importance and reflects the emerging challenge of the academic community and the chemical industry towards green chemistry. The design and development of more efficient synthetic processes is one of the major goals of green chemistry. Moreover, the integration of biocatalysis into chemical processes and the innovative potential of biotransformations in the promotion of the multistep catalytic concept, can contribute to the significantly improved process economy by avoiding time-, effort-, and solvent intensive steps. This innovative methodology offers great applications on Sustainable Chemistry.

This Special Issue on Biocatalysis and Biotransformations in Organic Synthesis will offer an attractive forum to present the synthetic potential of biocatalysis. I strongly encourage authors to submit papers for this Special Issue on BBOS, within the scope of Molecules. I hope that the topics covered will reflect the potential and the excitement of BBOS in the chemical community.

Ioulia Smonou
Guest Editor

Keywords

  • Biocatalysis
  • Enzymatic reactions
  • Biotransformations
  • Chemoenzymatic synthesis
  • Enantioselective synthesis
  • Cascade chemoenzymatic processes
  • Multi-step one-pot processes
  • New biocatalytic processes
  • Sustainable Chemistry
  • Multistep enzymatic transformations

Published Papers (3 papers)

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Research

Open AccessArticle Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine
Molecules 2012, 17(12), 13813-13824; doi:10.3390/molecules171213813
Received: 17 September 2012 / Revised: 15 November 2012 / Accepted: 16 November 2012 / Published: 22 November 2012
Cited by 5 | PDF Full-text (209 KB) | HTML Full-text | XML Full-text
Abstract
Lipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (acetate, butyrate, decanoate, laurate, palmitate). The
[...] Read more.
Lipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (acetate, butyrate, decanoate, laurate, palmitate). The transesterification activities of these immobilized enzymes were compared with commercially available lipases (lipase from hog pancreas, Aspergillus niger, Candida antarctica, Pseudomonas fluorescens). Lipase from Candida antarctica was found to be the most efficient enzyme regarding chemical yield of the desired products, while transesterification by lipase from Aspergillus niger resulted in lower yields. Full article
(This article belongs to the Special Issue Biocatalysis and Biotransformations in Organic Synthesis)
Open AccessArticle Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols
Molecules 2012, 17(11), 13045-13061; doi:10.3390/molecules171113045
Received: 26 September 2012 / Revised: 15 October 2012 / Accepted: 30 October 2012 / Published: 2 November 2012
Cited by 17 | PDF Full-text (1054 KB) | HTML Full-text | XML Full-text
Abstract
Sol-gel entrapment is an efficient immobilization technique that allows preparation of robust and highly stable biocatalysts. Lipase from Candida antarctica B was immobilized by sol-gel entrapment and by sol-gel entrapment combined with adsorption on Celite 545, using a ternary silane precursor system. After
[...] Read more.
Sol-gel entrapment is an efficient immobilization technique that allows preparation of robust and highly stable biocatalysts. Lipase from Candida antarctica B was immobilized by sol-gel entrapment and by sol-gel entrapment combined with adsorption on Celite 545, using a ternary silane precursor system. After optimization of the immobilization protocol, the best enzyme loading was 17.4 mg/g support for sol-gel entrapped lipase and 10.7 mg/g support for samples obtained by entrapment and adsorption. Sol-gel immobilized enzymes showed excellent values of enantiomeric ratio E and activity when ionic liquid 1-octyl-3-methyl-imidazolium tetrafluoroborate was used as additive. Immobilization increased the stability of the obtained biocatalysts in several organic solvents. Excellent operational stability was obtained for the immobilized lipase, maintaining unaltered catalytic activity and enantioselectivity during 15 reuse cycles. The biocatalysts were characterized using scanning electron microscopy (SEM) and fluorescence microscopy. The improved catalytic efficiency of entrapped lipases recommends their application for large-scale kinetic resolution of optically active secondary alcohols. Full article
(This article belongs to the Special Issue Biocatalysis and Biotransformations in Organic Synthesis)
Open AccessArticle Syntheses of Enantiopure Aliphatic Secondary Alcohols and Acetates by Bioresolution with Lipase B from Candida antarctica
Molecules 2012, 17(8), 8955-8967; doi:10.3390/molecules17088955
Received: 24 April 2012 / Revised: 27 June 2012 / Accepted: 3 July 2012 / Published: 26 July 2012
Cited by 11 | PDF Full-text (822 KB) | HTML Full-text | XML Full-text
Abstract
The lipase B from Candida antarctica (Novozym 435®, CALB) efficiently catalyzed the kinetic resolution of some aliphatic secondary alcohols: (±)-4-methylpentan-2-ol (1), (±)-5-methylhexan-2-ol (3), (±)-octan-2-ol (4), (±)-heptan-3-ol (5) and (±)-oct-1-en-3-ol (6). The
[...] Read more.
The lipase B from Candida antarctica (Novozym 435®, CALB) efficiently catalyzed the kinetic resolution of some aliphatic secondary alcohols: (±)-4-methylpentan-2-ol (1), (±)-5-methylhexan-2-ol (3), (±)-octan-2-ol (4), (±)-heptan-3-ol (5) and (±)-oct-1-en-3-ol (6). The lipase showed excellent enantioselectivities in the transesterifications of racemic aliphatic secondary alcohols producing the enantiopure alcohols (>99% ee) and acetates (>99% ee) with good yields. Kinetic resolution of rac-alcohols was successfully achieved with CALB lipase using simple conditions, vinyl acetate as acylating agent, and hexane as non-polar solvent. Full article
(This article belongs to the Special Issue Biocatalysis and Biotransformations in Organic Synthesis)

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