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Catalysts
Special Issues
Biocatalysis in Non-conventional Media
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Biocatalysis in Non-conventional Media

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

Deadline for manuscript submissions: closed (31 March 2023) | Viewed by 5748

Special Issue Editors

Prof. Dr. Francesco Molinari

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Guest Editor
Department of Food, Environmental and Nutritional Sciences (DeFENS), University of Milano, Milano, Italy
Interests: biocatalysis; fermentation; green chemistry
Prof. Dr. Sergio Riva

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Guest Editor
Consiglio Nazionale delle Ricerche, Rome, Italy
Interests: laccase; biocatalysis; oxidation; stereoselectivity; laccase-mediator systems; csp2-h bonds activation; radical c-o and c-c couplings; cycloadditions
Prof. Dr. Francesco Secundo

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Guest Editor
“Giulio Natta” Institute of Chemical Sciences and Technologies, National Research Council of Italy, I-20131 Milan, Italy
Interests: enzyme technologies; enzyme immobilization; biocatalysis in non-conventional media; biotransformations; protein conformation
Special Issues, Collections and Topics in MDPI journals
Prof. Daniela Ubiali

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Guest Editor
Department of Drug Sciences, University of Pavia, 27100 Pavia, Italy
Interests: biocatalysis; enzyme immobilization; circular bioeconomy
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Inspired by the 6th edition of the Biocatalysis in Non-Conventional Media (BNCM2021) held on 6–8 May 2021, we are pleased to guest edit a Special Issue collecting papers and/or reviews on the use of biocatalysts in non-conventional environments.

Starting in the 1980s, biocatalysis in non-conventional media has made various new powerful and sustainable synthetic strategies available for the preparation of compounds of interest for the agri-food, pharmaceutical, and polymers industries.

Even though the use of biocatalysts in non-conventional media might be considered a niche of biocatalysis, it has been growing as an area of fundamental and applied research thanks to the identification of:

i) New enzymes, more stable toward organic media;
ii) New enzyme formulations, evolving from crude enzyme powders to immobilized enzymes on various types of nanostructured supports;
iii) New types of non-conventional media, moving from “classical” organic solvents to green solvents and even more to solvent-free systems, from ionic liquids to deep eutectic solvents;
iv) New reaction setups, such as those developed in flow-chemistry systems.

Therefore, for this Special Issue, we welcome contributions on these topics, be they related to fundamental science or to practical applications.

Prof. Dr. Francesco Molinari
Prof. Dr. Sergio Riva
Prof. Dr. Francesco Secundo
Prof. Daniela Ubiali
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.

Published Papers (3 papers)

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Research

11 pages, 982 KiB  
Article
Regioselective Esterification of Cardiac Glycosides Catalyzed by Novozym 435 and Lipase PS in Organic Solvents
by Ivan Bassanini, Lucia Roncaglia, Bruno Danieli and Sergio Riva
Catalysts 2023, 13(5), 819; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13050819 - 28 Apr 2023
Viewed by 1048
Abstract
The enzymatic acetylation in the organic solvents of a number of the important bioactive cardiac glycosides was investigated. With the bufanolide proscillaridin A and the cardenolide lanatoside C, acylation, as expected, occurred at the secondary 4′-OH of the rhamnopyranosyl unit of the former [...] Read more.
The enzymatic acetylation in the organic solvents of a number of the important bioactive cardiac glycosides was investigated. With the bufanolide proscillaridin A and the cardenolide lanatoside C, acylation, as expected, occurred at the secondary 4′-OH of the rhamnopyranosyl unit of the former (by the action of Novozym 435 lipase) and the primary 6′′′′-OH of the terminal glucopyranosyl unit of the latter (best results obtained by the action of the lipase PS). Only lipase PS was found to be able to acylate the cardenolides digitoxin and digoxin at the 4‴-OH of their terminal digitoxose unit. The corresponding monoacetyl derivatives, both of which are commercialized drugs, could be isolated with good yields. The investigation of the Novozym 435-catalyzed acetylation of free D-digitoxose provided a possible explanation for the inability of this lipase to acylate digitoxin and digoxin. Full article
(This article belongs to the Special Issue Biocatalysis in Non-conventional Media)
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15 pages, 5467 KiB  
Article
Visualizing Hydrophobic and Hydrophilic Enzyme Interactions during Immobilization by Means of Infrared Microscopy
by Oliver Pauli, Achim Ecker, Alvaro Cruz-Izquierdo, Alessandra Basso and Simona Serban
Catalysts 2022, 12(9), 989; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12090989 - 01 Sep 2022
Cited by 4 | Viewed by 2133
Abstract
A novel Fourier transform infrared (FT-IR) microscopy method was developed and used to analyze the diffusion of lipase CalB in two different resins during immobilization. The method consisted of a streamlined sample preparation process and an automated transmission FT-IR microscopic measurement using a [...] Read more.
A novel Fourier transform infrared (FT-IR) microscopy method was developed and used to analyze the diffusion of lipase CalB in two different resins during immobilization. The method consisted of a streamlined sample preparation process and an automated transmission FT-IR microscopic measurement using a commercial benchtop device. The immobilization of CalB was performed on a hydrophobic resin containing aromatic groups (ECR1030M based on divinylbenzene) and on a hydrophilic resin containing ester groups and thus oxygen (ECR8204M based on methacrylate) and FT-IR revealed that the kinetic of immobilization and the distribution of the enzyme on the two resins were completely different. Furthermore, the technique revealed that CalB was immobilized on the external surface only in the case of the hydrophobic ECR1030M in a layer of about 50–70 µm, whereas when immobilized on the hydrophilic carrier ECR8204M the interaction of the enzyme with the carrier was uniform over the full diameter of the polymer bead. The enzyme activity however was higher on the hydrophobic support ECR1030M. Full article
(This article belongs to the Special Issue Biocatalysis in Non-conventional Media)
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10 pages, 1641 KiB  
Communication
Continuous Flow Glycolipid Synthesis Using a Packed Bed Reactor
by Rebecca Hollenbach, Delphine Muller, André Delavault and Christoph Syldatk
Catalysts 2022, 12(5), 551; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12050551 - 18 May 2022
Cited by 3 | Viewed by 1827
Abstract
Glycolipids are a class of biodegradable biosurfactants that are non-toxic and based on renewables, making them a sustainable alternative to petrochemical surfactants. Enzymatic synthesis allows a tailor-made production of these versatile compounds using sugar and fatty acid building blocks with rationalized structures for [...] Read more.
Glycolipids are a class of biodegradable biosurfactants that are non-toxic and based on renewables, making them a sustainable alternative to petrochemical surfactants. Enzymatic synthesis allows a tailor-made production of these versatile compounds using sugar and fatty acid building blocks with rationalized structures for targeted applications. Therefore, glycolipids can be comprehensively designed to outcompete conventional surfactants regarding their physicochemical properties. However, enzymatic glycolipid processes are struggling with both sugars and fatty acid solubilities in reaction media. Thus, continuous flow processes represent a powerful tool in designing efficient syntheses of sugar esters. In this study, a continuous enzymatic glycolipid production catalyzed by Novozyme 435® is presented as an unprecedented concept. A biphasic aqueous–organic system was investigated, allowing for the simultaneous solubilization of sugars and fatty acids. Owing to phase separation, the remaining non-acylated glucose was easily separated from the product stream and was refed to the reactor forming a closed-loop system. Productivity in the continuous process was higher compared to a batch one, with space–time yields of up to 1228 ± 65 µmol/L/h. A temperature of 70 °C resulted in the highest glucose-6-O-decanoate concentration in the Packed Bed Reactor (PBR). Consequently, the design of a continuous biocatalytic production is a step towards a more competitive glycolipid synthesis in the aim for industrialization. Full article
(This article belongs to the Special Issue Biocatalysis in Non-conventional Media)
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