Special Issue "Biocatalysis and Pharmaceuticals: A Smart Tool for Sustainable Development"

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: 28 February 2019

Special Issue Editor

Guest Editor
Prof. Andres R Alcantara

Department of Chemistry in Pharmaceutical Sciences, Pharmacy Faculty, Complutense University,Plaza de Ramon y Cajal, S/N University City, Madrid, Spain
Website | E-Mail
Interests: enzymatic synthesis of drugs and bioactive compounds; sustainable processes; biocatalysts upgrading; pharmaceutical industry

Special Issue Information

Dear Colleagues,

In the last years, the advances in bioinformatics, enzyme evolution or process intensification have enlarged the effectiveness of biotransformations, accelerating the rate at which new enzymes are becoming available, even for promiscuous activities not previously known. Thus, now it is possible to join the exquisite enzymatic precision and inherent sustainability associated to the employ of biocatalysts with the possibility of generating new and more robust biocatalysts, expanding the biocatalytic toolbox, moving inside a time scale more compatible with the demands of pharmaceutical industry. For these reasons, it seems clear that we are entering in a new scenario, in which biocatalysis will play an even more significant role in such a competitive and demanding industry.

This Special Issue aims to gather contributions from research groups, rather original research or up-to-date revisions, to illustrate recent advances in this fascinating area. This includes, but is not restricted to, the discovery of new enzymatic activities, the chemical or genetic modification of known biocatalysts for further application in the development of new drugs, and the implementation of biocatalyzed protocols to increase the sustainability in the synthesis of drugs and bioactive molecules.

Prof. Andres R Alcantara
Guest Editor

Manuscript Submission Information

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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. Catalysts is an international peer-reviewed open access monthly 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 1300 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

  • Biocatalysis
  • Biotransformations
  • Drug synthesis
  • Sustainable Chemistry
  • Biocatalyst engineering

Published Papers (3 papers)

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Research

Open AccessArticle Development of Biotransamination Reactions towards the 3,4-Dihydro-2H-1,5-benzoxathiepin-3-amine Enantiomers
Catalysts 2018, 8(10), 470; https://doi.org/10.3390/catal8100470
Received: 7 September 2018 / Revised: 9 October 2018 / Accepted: 16 October 2018 / Published: 19 October 2018
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Abstract
The stereoselective synthesis of chiral amines is an appealing task nowadays. In this context, biocatalysis plays a crucial role due to the straightforward conversion of prochiral and racemic ketones into enantiopure amines by means of a series of enzyme classes such as amine
[...] Read more.
The stereoselective synthesis of chiral amines is an appealing task nowadays. In this context, biocatalysis plays a crucial role due to the straightforward conversion of prochiral and racemic ketones into enantiopure amines by means of a series of enzyme classes such as amine dehydrogenases, imine reductases, reductive aminases and amine transaminases. In particular, the stereoselective synthesis of 1,5-benzoxathiepin-3-amines have attracted particular attention since they possess remarkable biological profiles; however, their access through biocatalytic methods is unexplored. Amine transaminases are applied herein in the biotransamination of 3,4-dihydro-2H-1,5-benzoxathiepin-3-one, finding suitable enzymes for accessing both target amine enantiomers in high conversion and enantiomeric excess values. Biotransamination experiments have been analysed, trying to optimise the reaction conditions in terms of enzyme loading, temperature and reaction times. Full article
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Graphical abstract

Open AccessArticle OcUGT1-Catalyzed Glucosylation of Sulfuretin Yields Ten Glucosides
Catalysts 2018, 8(10), 416; https://doi.org/10.3390/catal8100416
Received: 2 September 2018 / Revised: 20 September 2018 / Accepted: 20 September 2018 / Published: 25 September 2018
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Abstract
Sulfuretin glucosides are important sources of innovative drugs. However, few glucosides of sulfuretin have been observed in nature. Therefore, it is urgent to diversify sulfuretin glycosides. Herein, glycosyltransferase (GT)-catalyzed glycodiversification of sulfuretin was achieved. Specifically, a flavonoid GT designated as OcUGT1 was used
[...] Read more.
Sulfuretin glucosides are important sources of innovative drugs. However, few glucosides of sulfuretin have been observed in nature. Therefore, it is urgent to diversify sulfuretin glycosides. Herein, glycosyltransferase (GT)-catalyzed glycodiversification of sulfuretin was achieved. Specifically, a flavonoid GT designated as OcUGT1 was used as a biocatalyst for the glucosylation of sulfuretin with UDP-Glc. The OcUGT1-assisted glucosylation of sulfuretin yielded ten glycosylated products, including three monoglucosides, five diglucosides and two triglucosides. The three monoglucosides were thus identified to be sulfuretin 3′-, 4′- and 6-glucoside according to HR-ESI-TOFMS data and their coelution with respective standards. A major diglucoside was assigned as sulfuretin 4′,6-diglucoside by HR-ESI-TOFMS in conjunction with NMR analysis. The exact structure of the other four diglucosides was not well characterized due to their trace amount. However, they were reasonably inferred as sulfuretin 3′,6-diglucoside, sulfuretin 3′,4′-diglucoside and two disaccharide glucosides. In addition, the structural identification of the remaining two triglucosides was not performed because of their small amount. However, one of the triglucosides was deduced to be sulfuretin 3′,4′,6-triglucoside based on the catalytic behavior of OcUGT1. Of the ten sulfuretin glucosides, at least six were new compounds. This is the first time to obtain monoglucosides, diglucosides and triglucosides of sulfuretin simultaneously by a single glycosyltransferase. Full article
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Open AccessArticle Laccase Activity as an Essential Factor in the Oligomerization of Rutin
Catalysts 2018, 8(8), 321; https://doi.org/10.3390/catal8080321
Received: 9 July 2018 / Revised: 24 July 2018 / Accepted: 3 August 2018 / Published: 6 August 2018
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Abstract
The enzyme-mediated polymerization of bioactive phenolic compounds, such as the flavonoid rutin, has gained interest due to the enhanced physico-chemical and biological properties of the products, which increases their potential application as a nutraceutical. In this work, the influence of enzyme activity on
[...] Read more.
The enzyme-mediated polymerization of bioactive phenolic compounds, such as the flavonoid rutin, has gained interest due to the enhanced physico-chemical and biological properties of the products, which increases their potential application as a nutraceutical. In this work, the influence of enzyme activity on rutin oligomerization was evaluated in reactions with low (1000 U/L) and high (10,000 U/L) initial laccase activities. For both reactions, high molecular weight oligomer fractions showed better properties compared to lower weight oligomers. Products of the reaction with low laccase activity exhibited thermal stability and antioxidant potential similar to control reaction, but led to higher inhibitory activity of xanthine oxidase and apparent aqueous solubility. Oligomers obtained in the reaction with high laccase activity showed better apparent aqueous solubility but decreased biological activities and stability. Their low antioxidant activity was correlated with a decreased phenolic content, which could be attributed to the formation of several bonds between rutin molecules. Full article
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