New Potential Applications of Enzymes in Biocatalysis and Next Challenges for a Green Chemistry

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

Deadline for manuscript submissions: closed (20 December 2021) | Viewed by 15193

Special Issue Editors


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Guest Editor
Department of Chemistry, Physics and Environment, Dunarea de Jos University of Galati, 800201 Galati, Romania
Interests: organic compounds; plant extracts; bioactive compounds; polyphenols; essential oils; antioxidants; antimicrobials; cytotoxicity
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Guest Editor
Ecole Nationale Supérieure de Chimie de Rennes, Univ Rennes, CNRS, ISCR–UMR6226, F-35000 Rennes, France
Interests: microorganisms; microbial enzymes; whole cells biocatalysis; biotransformation; bioremediation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes, natural catalysts known for their catalytic efficiency, selectivity and high substrate specification, have been successfully explored in various biocatalytic processes for the synthesis of value-added chemicals for both pharmaceutical, food, and beverage fields as well as in enviromental applications such as enzymatic bioremediation and production of renewable and clean energies.   

Ezymes isolated/purified from different biological sources (animals, plants, and microorganisms) can now work actively, in vitro, in numerous biocatalytic reactions.  Enzyme-assisted reactions are safe for health and environmentally friendly due to the excellent selectivity of the substrate, thus reducing the number of by-products and also through achieving mild reaction conditions. By performing reactions in water under ambient conditions, both the use of organic solvents and energy consumption are minimized. Hence, biocatalysis has been recognized as a green technology.

This Special Issue of Catalysts will focus on research papers or reviews that reflect the state of research in the field of biocatalysis. The potential topics include but are not limited to the following: synthesis catalysed by enzymes, plant enzymes, whole cells or microorganisms as catalysts, enzymes in green chemistry reactions, mechanisms of biocatalytic synthesis, biocatalytic multi-component (MCRs) reactions, new sustainable biocatalytic reactions.

Prof. Dr. Rodica-Mihaela Dinicǎ
Dr. Lidia Favier
Guest Editors

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Keywords

  • biocatalysis
  • organic compounds synthesis
  • plant enzymes
  • microbial enzymes
  • immobilized enzymes
  • whole-cells biocatalysts
  • green chemistry
  • natural products
  • biotransformation
  • bioremediation

Published Papers (4 papers)

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Research

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12 pages, 11233 KiB  
Article
Structural and Biochemical Characterization of Endo-β-1,4-glucanase from Dictyoglomus thermophilum, a Hyperthermostable and Halotolerant Cellulase
by Rita Berisio, Giovanni Barra, Maria Romano, Flavia Squeglia and Alessia Ruggiero
Catalysts 2022, 12(3), 302; https://doi.org/10.3390/catal12030302 - 07 Mar 2022
Cited by 2 | Viewed by 1842
Abstract
Enzymatic conversion of polysaccharides in the lignocellulosic biomass is currently the subject of intensive research and will be a key technology in future biorefineries. Using a bioinformatics approach, we previously identified a putative endo-β-1,4-glucanase (DtCel5A) from Dictyoglomus thermophilum, a chemoorganotrophic and thermophilic [...] Read more.
Enzymatic conversion of polysaccharides in the lignocellulosic biomass is currently the subject of intensive research and will be a key technology in future biorefineries. Using a bioinformatics approach, we previously identified a putative endo-β-1,4-glucanase (DtCel5A) from Dictyoglomus thermophilum, a chemoorganotrophic and thermophilic bacterium. Here, we structurally and functionally characterize DtCel5A and show that it is endowed with remarkable thermal and chemical stability. The structural features of DtCel5A and of its complex with cellobiose have been investigated by combining X-ray crystallography and other biophysical studies. Importantly, biochemical assays show that DtCel5A retains its activity on cellulose at high temperatures and at elevated salt concentrations. These features make DtCel5A an enzyme with interesting biotechnological applications for biomass degradation. Full article
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19 pages, 3686 KiB  
Article
Synthesis of Indigo-Dyes from Indole Derivatives by Unspecific Peroxygenases and Their Application for In-Situ Dyeing
by René Ullrich, Marzena Poraj-Kobielska, Owik M. Herold-Majumdar, Jesper Vind and Martin Hofrichter
Catalysts 2021, 11(12), 1495; https://doi.org/10.3390/catal11121495 - 09 Dec 2021
Cited by 9 | Viewed by 5905
Abstract
Tyrian purple (also known as royal or imperial purple) is the oldest known commercial pigment and still one of the most expensive dyes, often associated with the wardrobes of clergy and royalty. It is a brominated derivative of indigo, a natural dye that [...] Read more.
Tyrian purple (also known as royal or imperial purple) is the oldest known commercial pigment and still one of the most expensive dyes, often associated with the wardrobes of clergy and royalty. It is a brominated derivative of indigo, a natural dye that has been used since 4000 BC. Moreover, just recently, the therapeutic value of indigoids for the treatment of several disorders was discovered. The manufacturing of indigo derivatives by the existing chemical routes has become increasingly uninteresting due to the use of aggressive reagents, expensive starting materials and high-energy costs. Thus, both dyestuff manufacturers and the pharmaceutical industry are interested in the development of gentle preparation methods of indigoids from simple precursors. Here, we describe a simple enzymatic method for the one-step synthesis of Tyrian purple and other indigo derivatives with fungal peroxygenases (UPO, EC 1.11.2.1). The reaction does not require complex co-substrates and works well in phosphate buffers with H2O2 (<0.1 wt%) and less than 5% (v/v) acetonitrile as co-solvent. We demonstrate the scaling up of the reaction to 10 Liters and established thereupon an environmentally friendly combined synthesis and in-situ dyeing process, further simplifying the manufacturing of vat-dyed fabrics. Eventually, we screened a number of halogen-substituted indoles in the search for novel indigo derivatives, which may be of interest for pharmaceutical and/or dyeing purposes. Full article
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Review

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17 pages, 2189 KiB  
Review
Apiose-Relevant Glycosidases
by Elena Karnišová Potocká, Mária Mastihubová and Vladimír Mastihuba
Catalysts 2021, 11(10), 1251; https://doi.org/10.3390/catal11101251 - 18 Oct 2021
Cited by 7 | Viewed by 2592
Abstract
Apiose is a branched pentose naturally occurring either as a component of the plant cell wall polysaccharides or as a sugar moiety present in numerous plant secondary metabolites such as flavonoid and phenylethanoid glycosides, substrates in plant defense systems or as glycosylated aroma [...] Read more.
Apiose is a branched pentose naturally occurring either as a component of the plant cell wall polysaccharides or as a sugar moiety present in numerous plant secondary metabolites such as flavonoid and phenylethanoid glycosides, substrates in plant defense systems or as glycosylated aroma precursors. The enzymes catalyzing hydrolysis of such apiosylated substances (mainly glycosidases specific towards apiose or acuminose) have promising applications not only in hydrolysis (flavor development), but potentially also in the synthesis of apiosides and apioglucosides with pharmaceutical relevance. This review summarizes the actual knowledge of glycosidases recognizing apiose and their potential application in biocatalysis. Full article
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11 pages, 2847 KiB  
Review
Research Progress in Enzymatic Synthesis of Vitamin E Ester Derivatives
by Zhiqiang Zou, Lingmei Dai, Dehua Liu and Wei Du
Catalysts 2021, 11(6), 739; https://doi.org/10.3390/catal11060739 - 16 Jun 2021
Cited by 13 | Viewed by 3923
Abstract
Vitamin E is easily oxidized by light, air, oxidizing agents and heat, limiting its application in many ways. Compared to vitamin E, vitamin E ester derivatives exhibit improved stability and a stronger antioxidant capacity, and even gain new biological functions. In recent years, [...] Read more.
Vitamin E is easily oxidized by light, air, oxidizing agents and heat, limiting its application in many ways. Compared to vitamin E, vitamin E ester derivatives exhibit improved stability and a stronger antioxidant capacity, and even gain new biological functions. In recent years, enzymatic synthesis of vitamin E ester derivatives has received increasing attention due to its environmental friendliness, high catalytic efficiency, and inherent selectivity. This paper reviews the related progress of lipase-mediated preparation of vitamin E ester derivatives. The function of different vitamin E ester derivatives, and the main factors influencing the enzymatic acylation process, including enzyme species, acyl donor and acceptor, reaction media and water activity, are summarized in this paper. Finally, the perspective of lipase-catalyzed synthesis of vitamin E ester derivatives is also discussed. Full article
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