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Recent Developments in Using Biocatalysts and Whole Cells for Organic Synthesis

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (15 October 2016) | Viewed by 11200

Special Issue Editor


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Guest Editor
Head of Organic Chemistry, Department of Chemistry, University of Bath, Bath BA27AY, UK
Interests: organic synthesis; novel synthetic transformations; catalysis; chemical sensing and medicinal chemistry

Special Issue Information

Dear Colleagues,

The use of biocatalysts and whole cells as efficient catalysts for organic transformations represents an extremely important strategy for the preparation of complex organic products, with many bioprocesses having been carried out on an industrial scale. Given their importance, this Special Issue invites submission of papers on new research that describes the application of biocatalysts/whole cells for the transformation of organic substrates into valuable organic products. Potential examples could include the use of biocatalysts/whole cells to transform prochiral substrates into chiral products, protocols for the kinetic resolution/desymmetrisation of racemic/meso substrates, selective protection/deprotection reactions of substrates containing multiple functional groups, and remote functionalisation reactions. Applications where molecular biology techniques have been used to improve the performance of biocatalysts, or produce new biocatalytic activities are particularly welcome, as are synthetic biology studies that afford new organisms capable of producing synthetically useful organic products. Reviews of specific areas of biocatalysis, biotransformations and synthetic biology applied to organic synthesis and perspectives on potential future applications will also be considered for publication.

Prof. Dr. Steven Bull
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Chemo-enzymatic synthesis
  • New biocatalytic transformations applied to organic synthesis
  • Biocatalytic protocols for the synthesis of chiral products
  • Kinetic resolution strategies
  • Desymmetrisation strategies
  • Protection/deprotection strategies
  • Biocatalytic coupling reactions
  • Remote functionalisation reactions
  • Technological developments (e.g. immobilisation/flow biocatalysis/ new reactor design, etc.)
  • Biocatalysis in organic solvents
  • Site-directed mutagenesis to improve biocatalyst performance
  • Directed evolution to improve biocatalytic activity/selectivity profiles
  • New screening techniques to identify useful biocatalytic activities
  • Whole cell biotransformations applied to organic synthesis
  • Identification of new enzymes/organisms with useful biocatalytic activity
  • Synthetic biology studies applied to the production of organic products

Published Papers (2 papers)

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Research

2405 KiB  
Article
Immobilization of Chlamydomonas reinhardtii CLH1 on APTES-Coated Magnetic Iron Oxide Nanoparticles and Its Potential in the Production of Chlorophyll Derivatives
by Chih-Chung Yen, Yao-Chen Chuang, Chia-Yun Ko, Long-Fang O. Chen, Sheau-Shyang Chen, Chia-Jung Lin, Yi-Li Chou and Jei-Fu Shaw
Molecules 2016, 21(8), 972; https://doi.org/10.3390/molecules21080972 - 26 Jul 2016
Cited by 11 | Viewed by 5897
Abstract
Recombinant Chlamydomonas reinhardtii chlorophyllase 1 (CrCLH1) that could catalyze chlorophyll hydrolysis to chlorophyllide and phytol in vitro was successfully expressed in Escherichia coli. The recombinant CrCLH1 was immobilized through covalent binding with a cubic (3-aminopropyl) triethoxysilane (APTES) coating on magnetic iron oxide [...] Read more.
Recombinant Chlamydomonas reinhardtii chlorophyllase 1 (CrCLH1) that could catalyze chlorophyll hydrolysis to chlorophyllide and phytol in vitro was successfully expressed in Escherichia coli. The recombinant CrCLH1 was immobilized through covalent binding with a cubic (3-aminopropyl) triethoxysilane (APTES) coating on magnetic iron oxide nanoparticles (MIONPs), which led to markedly improved enzyme performance and decreased biocatalyst costs for potential industrial application. The immobilized enzyme exhibited a high immobilization yield (98.99 ± 0.91 mg/g of gel) and a chlorophyllase assay confirmed that the immobilized recombinant CrCLH1 retained enzymatic activity (722.3 ± 50.3 U/g of gel). Biochemical analysis of the immobilized enzyme, compared with the free enzyme, showed higher optimal pH and pH stability for chlorophyll-a hydrolysis in an acidic environment (pH 3–5). In addition, compared with the free enzyme, the immobilized enzyme showed higher activity in chlorophyll-a hydrolysis in a high temperature environment (50–60 °C). Moreover, the immobilized enzyme retained a residual activity of more than 64% of its initial enzyme activity after 14 cycles in a repeated-batch operation. Therefore, APTES-coated MIONP-immobilized recombinant CrCLH1 can be repeatedly used to lower costs and is potentially useful for the industrial production of chlorophyll derivatives. Full article
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1795 KiB  
Article
Enzymatic Hydrolytic Resolution of Racemic Ibuprofen Ethyl Ester Using an Ionic Liquid as Cosolvent
by Tao Wei, Kunpeng Yang, Bing Bai, Jie Zang, Xuan Yu and Duobin Mao
Molecules 2016, 21(7), 905; https://doi.org/10.3390/molecules21070905 - 13 Jul 2016
Cited by 10 | Viewed by 5049
Abstract
The aim of this study was to develop an ionic liquid (IL) system for the enzymatic resolution of racemic ibuprofen ethyl ester to produce (S)-ibuprofen. Nineteen ILs were selected for use in buffer systems to investigate the effects of ILs as [...] Read more.
The aim of this study was to develop an ionic liquid (IL) system for the enzymatic resolution of racemic ibuprofen ethyl ester to produce (S)-ibuprofen. Nineteen ILs were selected for use in buffer systems to investigate the effects of ILs as cosolvents for the production of (S)-ibuprofen using thermostable esterase (EST10) from Thermotoga maritima. Analysis of the catalytic efficiency and conformation of EST10 showed that [OmPy][BF4] was the best medium for the EST10-catalyzed production of (S)-ibuprofen. The maximum degree of conversion degree (47.4%), enantiomeric excess of (S)-ibuprofen (96.6%) and enantiomeric ratio of EST10 (177.0) were achieved with an EST10 concentration of 15 mg/mL, racemic ibuprofen ethyl ester concentration of 150 mM, at 75 °C , with a reaction time of 10 h. The reaction time needed to achieve the highest yield of (S)-ibuprofen was decreased from 24 h to 10 h. These results are relevant to the proposed application of ILs as solvents for the EST10-catalyzed production of (S)-ibuprofen. Full article
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