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

Deadline for manuscript submissions: closed (10 March 2022) | Viewed by 9364

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Dr. Diána Balogh-Weiser

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Guest Editor

1. Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Budapest, Hungary
2. Department of Physical Chemistry and Materials Science, Budapest University of Technology and Economics, Budapest, Hungary
Interests: nanocatalysts; enzyme immobilization; carrier development; biocatalysis
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. László Poppe

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Guest Editor

Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Budapest, Hungary
Interests: organic chemistry; biocatalysis; stereoselective synthesis; enzyme development and application
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The importance of biocatalytic processes is growing rapidly in many fields due to the developing toolkits of biocatalysts enabled by sophistical analytical techniques uncovering unexplored natural biocatalysts and by the intensive growth of novel enzymes supported by recombinant techniques and directed evolution. Several synthetic and analytical processes rely on biocatalytic methods that provide unique and sustainable solutions in scientific or industrial fields or even in our everyday lives. Thus, the innovation of novel biocatalytic processes, especially for synthetic chemistry, is in the focus of attention.

This Special Issue on “Advanced Technologies for Biocatalytic Synthesis” welcomes the submission of original papers or reviews related to the field of biocatalysis, including the following topics: novel enzymes for biocatalytic processes, stereoselective synthesis catalyzed by biocatalysts, development of immobilized biocatalysts (enzyme or whole-cells), cascade biocatalytic synthesis, computational and/or experimental studies on enzyme mechanism, reactor design for biocatalytic processes, and integration of biocatalytic process in multi-level systems.

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

Manuscript Submission Information

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Keywords

Biocatalysis
Novel enzymes
Bioprocess engineering
Enzyme and whole-cell immobilization
Chemo-enzymatic synthesis

Published Papers (4 papers)

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Research

13 pages, 496 KiB

Open AccessArticle

Continuous Production of Fumaric Acid with Immobilised Rhizopus oryzae: The Role of pH and Urea Addition

by Reuben Marc Swart, Dominic Kibet Ronoh, Hendrik Brink and Willie Nicol

Catalysts 2022, 12(1), 82; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12010082 - 12 Jan 2022

Cited by 7 | Viewed by 1829

Abstract

Fumaric acid is widely used in the food and beverage, pharmaceutical and polyester resin industries. Rhizopus oryzae is the most successful microorganism at excreting fumaric acid compared to all known natural and genetically modified organisms. It has previously been discovered that careful control of the glucose feed rate can eliminate the by-product formation of ethanol. Two key parameters affecting fumaric acid excretion were identified, namely the medium pH and the urea feed rate. A continuous fermentation with immobilised R. oryzae was utilised to determine the effect of these parameters. It was found that the selectivity for fumaric acid production increased at high glucose consumption rates for a pH of 4, different from the trend for pH 5 and 6, achieving a yield of

0.93 gg^{- 1}

. This yield is higher than previously reported in the literature. Varying the urea feed rate to

0.255 m g L^{- 1} h^{- 1}

improved the yield of fumaric acid but experienced a lower glucose uptake rate compared to higher urea feed rates. An optimum region has been found for fumaric acid production at pH 4, a urea feed rate of

0.625 m g L^{- 1} h^{- 1}

and a glucose feed rate of

0.329 g L^{- 1} h^{- 1}

. Full article

(This article belongs to the Special Issue Advanced Technologies for Biocatalytic Synthesis)

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20 pages, 6578 KiB

Open AccessFeature PaperArticle

Transaminase Catalysis for Enantiopure Saturated Heterocycles as Potential Drug Scaffolds

by Ágnes Malta-Lakó, Fangyi Zhang, Ricardo Mendonça and László Poppe

Catalysts 2021, 11(12), 1501; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11121501 - 10 Dec 2021

Cited by 1 | Viewed by 2357

Abstract

As efforts in rational drug design are driving the pharmaceutical industry towards more complex molecules, the synthesis and production of these new drugs can benefit from new reaction routes. In addition to the introduction of new centers of asymmetry, complexity can be also increased by ring saturation, which also provides improved developability measures. Therefore, in this report, our aim was to develop transaminase (TA)-catalyzed asymmetric synthesis of a new group of potential chiral drug scaffolds comprising a saturated amine heterocycle backbone and an asymmetric primary amine sidechain (55a–g). We screened the Codex^® Amine Transaminase Kit of 24 transaminases with the morpholine containing ketone 57a, resulting in one (R)-selective TA and three (S)-selective TAs operating at 100 mM substrate concentration and 25 v/v% isopropylamine (IPA) content. The optimized reaction conditions were than applied for asymmetric transamination of further six ketones (57b–g) containing various amine heterocycles, in which a strong effect of the substitution pattern of the γ-position relative to the substituted N-atom could be observed. Mediated by the most enantiotope selective (S)-TAs in scaled-up process, the (S)-amines [(S)-55a–g] were isolated with moderate-to-excellent yields (47–94%) in enantiopure form (>99% ee). Full article

(This article belongs to the Special Issue Advanced Technologies for Biocatalytic Synthesis)

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14 pages, 13172 KiB

Open AccessFeature PaperArticle

Entrapment of Phenylalanine Ammonia-Lyase in Nanofibrous Polylactic Acid Matrices by Emulsion Electrospinning

by Gábor Koplányi, Evelin Sánta-Bell, Zsófia Molnár, Gergő Dániel Tóth, Muriel Józó, András Szilágyi, Ferenc Ender, Béla Pukánszky, Beáta G. Vértessy, László Poppe and Diána Balogh-Weiser

Catalysts 2021, 11(10), 1149; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11101149 - 25 Sep 2021

Cited by 6 | Viewed by 1990

Abstract

Immobilization of the recombinant, plant-derived Petroselinum crispum phenylalanine ammonia lyase (PcPAL) in electrospun matrices have the potential to create promising, easy-to-use biocatalysts. Polylactic acid (PLA) a biologically inert, commercial biopolymer, was chosen as the material of the carrier system. PLA could be electrospun properly only from water-immiscible organic solvents, which limits its application as a carrier of sensitive biological objects. The emulsion electrospinning is a proper solution to overcome this issue using non-ionic emulsifiers with different hydrophilic-lipophilic balance (HLB) values. The stabilized emulsion could protect the sensitive PcPAL dissolved in the aqueous buffer phase and improve fiber formation, plus help to keep the biocatalytic activity of enzymes. In this study, the first approach is described to produce PLA nanofibers containing PcPAL enzymes by emulsion electrospinning and to use the resulted biocatalyst in the ammonia elimination reaction from l-phenylalanine. Full article

(This article belongs to the Special Issue Advanced Technologies for Biocatalytic Synthesis)

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13 pages, 3471 KiB

Open AccessFeature PaperArticle

Magnetically Agitated Nanoparticle-Based Batch Reactors for Biocatalysis with Immobilized Aspartate Ammonia-Lyase

by Ali Obaid Imarah, Pál Csuka, Naran Bataa, Balázs Decsi, Evelin Sánta-Bell, Zsófia Molnár, Diána Balogh-Weiser and László Poppe

Catalysts 2021, 11(4), 483; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11040483 - 09 Apr 2021

Cited by 6 | Viewed by 2402

Abstract

In this study, we investigated the influence of different modes of magnetic mixing on effective enzyme activity of aspartate ammonia-lyase from Pseudomonas fluorescens immobilized onto epoxy-functionalized magnetic nanoparticles by covalent binding (AAL-MNP). The effective specific enzyme activity of AAL-MNPs in traditional shake vial method was compared to the specific activity of the MNP-based biocatalyst in two devices designed for magnetic agitation. The first device agitated the AAL-MNPs by moving two permanent magnets at two opposite sides of a vial in x-axis direction (being perpendicular to the y-axis of the vial); the second device unsettled the MNP biocatalyst by rotating the two permanent magnets around the y-axis of the vial. In a traditional shake vial, the substrate and biocatalyst move in the same direction with the same pattern. In magnetic agitation modes, the MNPs responded differently to the external magnetic field of two permanent magnets. In the axial agitation mode, MNPs formed a moving cloud inside the vial, whereas in the rotating agitation mode, they formed a ring. Especially, the rotating agitation of the MNPs generated small fluid flow inside the vial enabling the mixing of the reaction mixture, leading to enhanced effective activity of AAL-MNPs compared to shake vial agitation. Full article

(This article belongs to the Special Issue Advanced Technologies for Biocatalytic Synthesis)

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