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Catalysts
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Enzymes in Materials Science
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Enzymes in Materials Science

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

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 6118

Special Issue Editor

Prof. Dr. Oliver Strube

E-Mail Website
Guest Editor
Department of Chemistry–Biobased and Bioinspired Materials, Paderborn University, Warburger Street 100, 33098 Paderborn, Germany
Interests: bioinspired materials; coatings technology; reaction engineering

Special Issue Information

Dear Colleagues,

In recent decades, the utilization of enzymes for special synthetic purposes has become more and more popular in numerous fields of applied sciences. The number of commercially available enzymes is continuously increasing and novel methods in biotechnology allow for the production of pure and highly reactive enzymes at acceptable prices.

The examples of technical applications for enzymes are ever increasing, especially in food processing, medical applications and chemical syntheses, such as the production of biopolymers from natural resources.

In the wake of these developments, the research on bioinspired and biomimetic materials has also had an enormous trajectory, and especially the value of enzymes in materials science has been widely acknowledged in this context. Nowadays, countless high-impact research papers are published every year, which highlight the near endless capabilities of enzymatic catalysis towards advanced materials.

With this Special Issue, we aim to bring together all relevant fields of research to give additional momentum and visibility to the manifold approaches of enzyme application in cutting-edge materials science. This includes the application of inherent enzymatic activity, e.g., at surfaces or in coatings, as well as bioinspired materials buildup, guided by enzymes. Additional important aspects are basic research challenges, like the availability of enzymes at acceptable costs, the examination of enzymatic reaction pathways and the understanding of natural archetypes.

Prof. Dr. Oliver Strube
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. 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

  • Bioinspired materials science
  • Biomimetic materials
  • Enzyme immobilization
  • Biocatalytic surfaces and coatings
  • Enzyme production routes
  • Technical enzymes
  • Surface analysis
  • Biocatalytic synthesis of materials

Published Papers (3 papers)

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Research

14 pages, 2143 KiB  
Article
Rheological Characterization and Quality of Emulsions Based on Fats Produced during the Reaction Catalyzed by Immobilized Lipase from Rhizomucor Miehei
by Małgorzata Kowalska, Marcin Krzton-Maziopa, Anna Krzton-Maziopa, Anna Zbikowska and Jerzy Szakiel
Catalysts 2022, 12(6), 649; https://doi.org/10.3390/catal12060649 - 13 Jun 2022
Cited by 1 | Viewed by 1533
Abstract
It has been shown that structured lipids, formed in the process of enzymatic modification of natural hard fat with walnut oil, are capable of stabilizing emulsion systems without the need to add additional emulsifiers. This is especially true for emulsions containing fat formed [...] Read more.
It has been shown that structured lipids, formed in the process of enzymatic modification of natural hard fat with walnut oil, are capable of stabilizing emulsion systems without the need to add additional emulsifiers. This is especially true for emulsions containing fat formed during enzymatic modification when the amount of added water to the reaction catalyst was in the range of 12–16 wt%. Physicochemical evaluations, i.e., the average particle size, its growth, distribution, and dispersity coefficient, were comparable with the reference emulsion where the emulsifier was lecithin, well-known for its emulsifying properties. Microstructure studies also confirmed the above observations. Rheological studies performed on a set of emulsions containing structured lipids of variable composition confirmed that interesterified lipid blends can be directly utilized as a fat base in the preparation of stable emulsions. The consistency, thixotropic behavior, long-term shelf life, and thermal stability of these emulsions were found to be comparable to systems stabilized with conventional emulsifiers, i.e., sunflower lecithine. Our approach offers the opportunity for the preparation of stable emulsion systems, free from additional emulsifiers, for the food or cosmetics industry, which is extremely important from the point of view of the preparation of products free from allergens. Full article
(This article belongs to the Special Issue Enzymes in Materials Science)
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9 pages, 2042 KiB  
Article
A Multicomponent Butyrylcholinesterase Preparation for Enzyme Inhibition-Based Assay of Organophosphorus Pesticides
by Victoria I. Lonshakova-Mukina, Elena N. Esimbekova and Valentina A. Kratasyuk
Catalysts 2022, 12(6), 643; https://doi.org/10.3390/catal12060643 - 12 Jun 2022
Cited by 4 | Viewed by 1729
Abstract
A new method of producing butyrylcholinesterase (BChE) preparations, stable in storage and use, has been proposed. The BChE preparation is the enzyme co-immobilized with 0.2 M 5-5′-dithiobis (2-nitrobenzoic acid) in starch or gelatin gel. All experimental preparations retain enzyme activity for at least [...] Read more.
A new method of producing butyrylcholinesterase (BChE) preparations, stable in storage and use, has been proposed. The BChE preparation is the enzyme co-immobilized with 0.2 M 5-5′-dithiobis (2-nitrobenzoic acid) in starch or gelatin gel. All experimental preparations retain enzyme activity for at least 300 d. The preparations based on gelatin gel show higher activity but lower sensitivity to the toxicants tested in this study compared to the starch gel-based preparations. A method has been proposed for integrated detection of anti-cholinesterase substances in aqueous solutions using the experimental preparation with immobilized BChE. After the additional incubation of the preparation with the immobilized enzyme in the solution of the analyte, the detection limits of malathion and pirimiphos-methyl determined using the IC20 values were below their maximum allowable concentrations—0.005 µM and 0.03 µM, respectively. Full article
(This article belongs to the Special Issue Enzymes in Materials Science)
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12 pages, 2971 KiB  
Article
Highly Sensitive Amperometric Sensor Based on Laccase-Mimicking Metal-Based Hybrid Nanozymes for Adrenaline Analysis in Pharmaceuticals
by Olha Demkiv, Nataliya Stasyuk, Galina Gayda and Mykhailo Gonchar
Catalysts 2021, 11(12), 1510; https://doi.org/10.3390/catal11121510 - 11 Dec 2021
Cited by 5 | Viewed by 2220
Abstract
Nanozymes are nanomaterials which exhibit artificial enzymatic activities and are considered as alternatives to natural enzymes. They are characterized by good catalytic activity and high stability, as well as ease and low cost of preparation. In this study, the mimetics of laccase or [...] Read more.
Nanozymes are nanomaterials which exhibit artificial enzymatic activities and are considered as alternatives to natural enzymes. They are characterized by good catalytic activity and high stability, as well as ease and low cost of preparation. In this study, the mimetics of laccase or “nanolaccases” (NLacs) were synthesized by a simple method of chemical reduction of transition metal salts. The NLacs were tested for their catalytic activity in solution and on the electrode surface. The most effective NLacs, namely nAuCePt and nPtFe, were found to possess excellent laccase-like activities capable of oxidizing the endocrine hormone adrenaline (AD). These NLacs were characterized in detail and used for the development of amperometric sensors for AD determination. The amperometric sensors containing the best NLacs, as well as a natural fungal laccase, were constructed. The most effective nAuCePt-containing sensor had good specificity in relation to AD and improved analytical characteristics. It possessed a 384-fold higher sensitivity than adrenaline (230,137 A·M−1·m−2), a 64-fold lower limit of detection (0.025 µM), and a broader linear range (0.085–45 µM) in comparison with the sensor based on natural laccase. The constructed nAuCePt-containing sensor was successfully used for AD analysis in pharmaceutical formulation. Full article
(This article belongs to the Special Issue Enzymes in Materials Science)
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