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Journals
Catalysts
Special Issues
Enzymatic Functions for Novel Technologies—from Synthetic to Medicinal Uses
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Enzymatic Functions for Novel Technologies—from Synthetic to Medicinal Uses

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (30 June 2023) | Viewed by 2526

Special Issue Editors

Dr. Diána Balogh-Weiser

E-Mail Website
Guest Editor
1. Department of Physical Chemistry and Materials Science, Budapest University of Technology and Economics, Műegyetem rkp. 3, 1111 Budapest, Hungary
2. Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, 1111 Budapest, Hungary
Interests: nanocarriers; enzymes; biotransformations; biomedical engineering; enzyme replacement therapies
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. László Poppe

E-Mail Website
Guest Editor
Bioorganic Chemistry Group, Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Budapest, Hungary
Interests: biocatalysis; stereoselective synthesis; immobilization of biocatalysts; flow chemistry and biocatalysis; enzyme mechanisms
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue is concerned with biocatalytic processes with enzymes, proteins, and cells; these represent novel approaches for the application of enzymatic functions. The scope of this Issue includes applications such as selective biocatalytic synthesis, analysis, as well as natural and unnatural biotransformations related to the field of preparative chemistry, bioanalysis and medicinal chemistry.

Original articles and reviews related to the field of biocatalysis are welcome in this Special Issue.

Dr. Diána Balogh-Weiser
Prof. Dr. László Poppe
Guest Editors

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. 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 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

  • enzymatic catalysis
  • biotransformation
  • selective reactions
  • enzymatic functions

Published Papers (1 paper)

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Research

16 pages, 3122 KiB  
Article
A Convenient U-Shape Microreactor for Continuous Flow Biocatalysis with Enzyme-Coated Magnetic Nanoparticles-Lipase-Catalyzed Enantiomer Selective Acylation of 4-(Morpholin-4-yl)butan-2-ol
by Ali O. Imarah, Fausto M. W. G. Silva, László Tuba, Ágnes Malta-Lakó, József Szemes, Evelin Sánta-Bell and László Poppe
Catalysts 2022, 12(9), 1065; https://doi.org/10.3390/catal12091065 - 17 Sep 2022
Cited by 9 | Viewed by 2233
Abstract
This study implements a convenient microreactor for biocatalysis with enzymes immobilized on magnetic nanoparticles (MNPs). The enzyme immobilized onto MNPs by adsorption or by covalent bonds was lipase B from Candida antarctica (CaLB). The MNPs for adsorption were obtained by covering the magnetite [...] Read more.
This study implements a convenient microreactor for biocatalysis with enzymes immobilized on magnetic nanoparticles (MNPs). The enzyme immobilized onto MNPs by adsorption or by covalent bonds was lipase B from Candida antarctica (CaLB). The MNPs for adsorption were obtained by covering the magnetite core with a silica shell and later with hexadecyltrimethoxysilane, while for covalent immobilization, the silica-covered MNPs were functionalized by a layer forming from mixtures of hexadecyl- and 3-(2-aminoethylamino)propyldimethoxymethylsilanes in 16:1 molar ratio, which was further activated with neopentyl glycol diglycidyl ether (NGDE). The resulting CaLB-MNPs were tested in a convenient continuous flow system, created by 3D printing to hold six adjustable permanent magnets beneath a polytetrafluoroethylene tube (PTFE) to anchor the MNP biocatalyst inside the tube reactor. The anchored CaLB-MNPs formed reaction chambers in the tube for passing the fluid through and above the MNP biocatalysts, thus increasing the mixing during the fluid flow and resulting in enhanced activity of CaLB on MNPs. The enantiomer selective acylation of 4-(morpholin-4-yl)butan-2-ol (±)-1, being the chiral alcohol constituent of the mucolytic drug Fedrilate, was carried out by CaLB-MNPs in the U-shape reactor. The CaLB-MNPs in the U-shape reactor were compared in batch reactions to the lyophilized CaLB and to the CaLB-MNPs using the same reaction composition, and the same amounts of CaLB showed similar or higher activity in flow mode and superior activity as compared to the lyophilized powder form. The U-shape permanent magnet design represents a general and easy-to-access implementation of MNP-based flow microreactors, being useful for many biotransformations and reducing costly and time-consuming downstream processes. Full article
(This article belongs to the Special Issue Enzymatic Functions for Novel Technologies—from Synthetic to Medicinal Uses)
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