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Enzymes in Biosynthesis and Biocatalysis
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Enzymes in Biosynthesis and Biocatalysis

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: 31 May 2024 | Viewed by 5063

Special Issue Editors

Dr. Lindomar Alberto Lerin

E-Mail Website
Guest Editor
Department of Chemical, Pharmaceutical and Agricultural Sciences, University of Ferrara, Ferrara, Italy
Interests: biotechnological processes; enzyme; lipase; bioreactor enzymatic; optimization processes; esterification
Special Issues, Collections and Topics in MDPI journals
Dr. Daniela Remonatto

E-Mail Website
Guest Editor
Department of Bioprocesses and Biotechnology Engineering, São Paulo State University, Araraquara, Brazil
Interests: lipases; enzymes immobilization; biotechnological processes; bioreactor enzymatic; fermentative processes

Special Issue Information

Dear Colleagues,

Biocatalysis is an exponentially growing area concerned with the biosynthesis of compounds that have aroused great interest in the market, especially the pharmaceutical, food, cosmetic, and fine chemical industries. This aligns with the growing demand for natural products and/or ingredients obtained by processes with a low environmental impact. Enzymes play a crucial role in the biosynthesis of high-added-value compounds that can be recognized as natural. In addition, they represent a powerful tool in green chemistry, minimizing energy consumption, and reducing the generation of effluents, perfectly aligning with the circular economy and sustainable development. Despite these advantages, there are many challenges regarding the application of biocatalysts. Efforts are still necessary to develop biocatalysts with high stability, longer half-life, and lower economic impact. To overcome current challenges, research in different areas of enzymology, such as the search for new enzymes with different abilities, new immobilization methods and more economical carriers, the optimization of established processes, the development of new enzymatic biosynthetic routes of biomolecules and the use of alternative substrates in reactions (e.g., agro-industrial residues), must be constant and the future looks promising.

Dr. Lindomar Alberto Lerin
Dr. Daniela Remonatto
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. Molecules is an international peer-reviewed open access semimonthly 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

  • biocatalysis
  • biosynthesis
  • green processes
  • enzyme
  • renewable sources
  • immobilization
  • enzymatic synthesis

Published Papers (5 papers)

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Research

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19 pages, 3472 KiB  
Article
Synthesis and Bioactive Properties of the Novel Coloured Compound Obtained via the Laccase-Mediated Transformation of 5-Aminosalicylic Acid
by Jolanta Polak, Marcin Grąz, Katarzyna Szałapata, Justyna Kapral-Piotrowska, Kamila Wlizło, Marcin Polak and Anna Jarosz-Wilkołazka
Molecules 2024, 29(6), 1310; https://doi.org/10.3390/molecules29061310 - 15 Mar 2024
Viewed by 514
Abstract
Biocatalysis processes based on oxidoreductases, such as fungal laccase, are important for discovering new organic compounds with broad structures and potential applications. They include bioactive compounds, which can be obtained through laccase-mediated oxidation of organic substrates having hydroxyl and/or amino groups especially, e.g., [...] Read more.
Biocatalysis processes based on oxidoreductases, such as fungal laccase, are important for discovering new organic compounds with broad structures and potential applications. They include bioactive compounds, which can be obtained through laccase-mediated oxidation of organic substrates having hydroxyl and/or amino groups especially, e.g., 5-aminosalicylic acid (5-ASA) is characterised for its potential for oxidation by a fungal laccase obtained from a Cerrena unicolor strain. The biotransformation process was optimised in terms of the buffer and co-solvent concentration, buffer pH value, and laccase activity. Selected crude dyes were analysed for their bioactive properties, toxicity, and suitability for the dyeing of wool fibres. The data obtained clearly indicated that a low concentration of the reaction buffer in the pH range from 5 to 6 and in the presence of 10% acetonitrile increased the rate of substrate oxidation and the amount of the product formed. The red-brown compound obtained via laccase-mediated oxidation of 5-aminosalicylic acid showed antioxidant properties and unique antimicrobial activity against Staphylococcus aureus and Staphylococcus epidermidis strains with the MIC value of 0.125 mg/mL detected for the purest dye. In addition, it was reported to have good wool fibre dyeing properties and no irritant effect after patch tests on a selected group with increased skin sensitivity. Full article
(This article belongs to the Special Issue Enzymes in Biosynthesis and Biocatalysis)
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13 pages, 641 KiB  
Article
Selective Wine Aroma Enhancement through Enzyme Hydrolysis of Glycosidic Precursors
by José Manuel Rodríguez-Nogales, Encarnación Fernández-Fernández, Violeta Ruipérez and Josefina Vila-Crespo
Molecules 2024, 29(1), 16; https://doi.org/10.3390/molecules29010016 - 19 Dec 2023
Viewed by 734
Abstract
Selective enhancement of wine aroma was achieved using a broad spectrum of exogenous glycosidases. Eight different enzyme preparations were added to Verdejo wine, resulting in an increase in the levels of varietal volatile compounds compared to the control wine after 15 days of [...] Read more.
Selective enhancement of wine aroma was achieved using a broad spectrum of exogenous glycosidases. Eight different enzyme preparations were added to Verdejo wine, resulting in an increase in the levels of varietal volatile compounds compared to the control wine after 15 days of treatment. The enzyme preparations studied were robust under winemaking conditions (sulfur dioxide, reducing sugars, and alcohol content), and no inhibition of β-glucosidase activity was observed. Significant differences were detected in four individual terpenes (α-terpineol, terpinen-4-ol, α-pinene, and citronellal) and benzyl alcohol in all the treated wines compared to the control wine, contributing to the final wine to varying degrees. In addition, a significant increase in the other aromatic compounds was observed, which showed different patterns depending on the enzyme preparation that was tested. The principal component analysis of the data revealed the possibility of modulating the different aromatic profiles of the final wines depending on the enzyme preparation used. Taking these results into account, enhancement of the floral, balsamic, and/or fruity notes of wines is possible by using a suitable commercial enzyme preparation. Full article
(This article belongs to the Special Issue Enzymes in Biosynthesis and Biocatalysis)
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24 pages, 2343 KiB  
Article
Statistical Improvement of rGILCC 1 and rPOXA 1B Laccases Activity Assay Conditions Supported by Molecular Dynamics
by María P. C. Mora-Gamboa, María C. Ferrucho-Calle, Leidy D. Ardila-Leal, Lina M. Rojas-Ojeda, Johan F. Galindo, Raúl A. Poutou-Piñales, Aura M. Pedroza-Rodríguez and Balkys E. Quevedo-Hidalgo
Molecules 2023, 28(21), 7263; https://doi.org/10.3390/molecules28217263 - 25 Oct 2023
Viewed by 852
Abstract
Laccases (E.C. 1.10.3.2) are glycoproteins widely distributed in nature. Their structural conformation includes three copper sites in their catalytic center, which are responsible for facilitating substrate oxidation, leading to the generation of H2O instead of H2O2. The [...] Read more.
Laccases (E.C. 1.10.3.2) are glycoproteins widely distributed in nature. Their structural conformation includes three copper sites in their catalytic center, which are responsible for facilitating substrate oxidation, leading to the generation of H2O instead of H2O2. The measurement of laccase activity (UL−1) results may vary depending on the type of laccase, buffer, redox mediators, and substrates employed. The aim was to select the best conditions for rGILCC 1 and rPOXA 1B laccases activity assay. After sequential statistical assays, the molecular dynamics proved to support this process, and we aimed to accumulate valuable insights into the potential application of these enzymes for the degradation of novel substrates with negative environmental implications. Citrate buffer treatment T2 (CB T2) (pH 3.0 ± 0.2; λ420nm, 2 mM ABTS) had the most favorable results, with 7.315 ± 0.131 UL−1 for rGILCC 1 and 5291.665 ± 45.83 UL−1 for rPOXA 1B. The use of citrate buffer increased the enzyme affinity for ABTS since lower Km values occurred for both enzymes (1.49 × 10−2 mM for rGILCC 1 and 3.72 × 10−2 mM for rPOXA 1B) compared to those obtained in acetate buffer (5.36 × 10−2 mM for rGILCC 1 and 1.72 mM for rPOXA 1B). The molecular dynamics of GILCC 1–ABTS and POXA 1B–ABTS showed stable behavior, with root mean square deviation (RMSD) values not exceeding 2.0 Å. Enzyme activities (rGILCC 1 and rPOXA 1B) and 3D model–ABTS interactions (GILCC 1–ABTS and POXA 1B–ABTS) were under the strong influence of pH, wavelength, ions, and ABTS concentration, supported by computational studies identifying the stabilizing residues and interactions. Integration of the experimental and computational approaches yielded a comprehensive understanding of enzyme–substrate interactions, offering potential applications in environmental substrate treatments. Full article
(This article belongs to the Special Issue Enzymes in Biosynthesis and Biocatalysis)
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18 pages, 3144 KiB  
Article
Solvent-Free Enzymatic Synthesis of Dietary Triacylglycerols from Cottonseed Oil in a Fluidized Bed Reactor
by Daniela Remonatto, Núbia Santaella, Lindomar Alberto Lerin, Juliana Cristina Bassan, Marcel Otávio Cerri and Ariela Veloso de Paula
Molecules 2023, 28(14), 5384; https://doi.org/10.3390/molecules28145384 - 13 Jul 2023
Cited by 2 | Viewed by 1230
Abstract
The synthesis of structured lipids with nutraceutical applications, such as medium-long-medium (MLM) triacylglycerols, via modification of oils and fats represents a challenge for the food industry. This study aimed to synthesize MLM-type dietary triacylglycerols by enzymatic acidolysis of cottonseed oil and capric acid [...] Read more.
The synthesis of structured lipids with nutraceutical applications, such as medium-long-medium (MLM) triacylglycerols, via modification of oils and fats represents a challenge for the food industry. This study aimed to synthesize MLM-type dietary triacylglycerols by enzymatic acidolysis of cottonseed oil and capric acid (C10) catalyzed by Lipozyme RM IM (lipase from Rhizomucor miehei) in a fluidized bed reactor (FBR). After chemical characterization of the feedstock and hydrodynamic characterization of the reactor, a 22 central composite rotatable design was used to optimize capric acid incorporation. The independent variables were cycle number (20–70) and cottonseed oil/capric acid molar ratio (1:2–1:4). The temperature was set at 45 °C. The best conditions, namely a 1:4 oil/acid molar ratio and 80 cycles (17.34 h), provided a degree of incorporation of about 40 mol%, as shown by compositional analysis of the modified oil. Lipozyme RM IM showed good operational stability (kd = 2.72 × 10−4 h−1, t1/2 = 2545.78 h), confirming the good reuse capacity of the enzyme in the acidolysis of cottonseed oil with capric acid. It is concluded that an FBR configuration is a promising alternative for the enzymatic synthesis of MLM triacylglycerols. Full article
(This article belongs to the Special Issue Enzymes in Biosynthesis and Biocatalysis)
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18 pages, 25594 KiB  
Review
Advances in 4-Hydroxyphenylacetate-3-hydroxylase Monooxygenase
by Kai Yang, Qianchao Zhang, Weirui Zhao, Sheng Hu, Changjiang Lv, Jun Huang, Jiaqi Mei and Lehe Mei
Molecules 2023, 28(18), 6699; https://doi.org/10.3390/molecules28186699 - 19 Sep 2023
Cited by 1 | Viewed by 1168
Abstract
Catechols have important applications in the pharmaceutical, food, cosmetic, and functional material industries. 4-hydroxyphenylacetate-3-hydroxylase (4HPA3H), a two-component enzyme system comprising HpaB (monooxygenase) and HpaC (FAD oxidoreductase), demonstrates significant potential for catechol production because it can be easily expressed, is highly active, and exhibits [...] Read more.
Catechols have important applications in the pharmaceutical, food, cosmetic, and functional material industries. 4-hydroxyphenylacetate-3-hydroxylase (4HPA3H), a two-component enzyme system comprising HpaB (monooxygenase) and HpaC (FAD oxidoreductase), demonstrates significant potential for catechol production because it can be easily expressed, is highly active, and exhibits ortho-hydroxylation activity toward a broad spectrum of phenol substrates. HpaB determines the ortho-hydroxylation efficiency and substrate spectrum of the enzyme; therefore, studying its structure–activity relationship, improving its properties, and developing a robust HpaB-conducting system are of significance and value; indeed, considerable efforts have been made in these areas in recent decades. Here, we review the classification, molecular structure, catalytic mechanism, primary efforts in protein engineering, and industrial applications of HpaB in catechol synthesis. Current trends in the further investigation of HpaB are also discussed. Full article
(This article belongs to the Special Issue Enzymes in Biosynthesis and Biocatalysis)
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