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Biomolecules
Special Issues
Recent Advances in the Enzymatic Synthesis of Bioactive Compounds
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Recent Advances in the Enzymatic Synthesis of Bioactive Compounds

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Natural and Bio-derived Molecules".

Deadline for manuscript submissions: 30 June 2025 | Viewed by 2757

Special Issue Editor

Dr. Bartłomiej Zieniuk

E-Mail Website
Guest Editor
Department of Chemistry, Institute of Food Sciences, Warsaw University of Life Sciences, Warsaw, Poland
Interests: lipase-catalyzed ester synthesis; lipophilization; enzymatic (trans)esterification; whole-cell modification of phenolic compounds; microbiology; yarrowia lipolytica; lipases biosynthesis; antimicrobial and antioxidant activities of phenolic compounds; microbial enzymes
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Catalysts primarily function by reducing the activation energy, which, in turn, increases the reaction rate. Enzymes, thus biocatalysts, which are derived from living organisms, are mostly macromolecular proteins that perform specific functions and are responsible for the proper functioning of living beings. Enzymes or microorganisms producing appropriate enzymes have been used since ancient times, often without conscious awareness. These biomolecules have been widely applied in various industries for many years, and it is difficult to imagine life without them today.

Biocatalysis and biotransformation approaches result in changes in the physicochemical properties and biological activity of the compounds. Enzymes are often utilized to create new derivatives with fascinating properties such as anti-cancer, antibacterial, and antiviral activities, which can also have beneficial health effects.

The current Special Issue aims to show the recent advances in enzymes and their applications in food technology, biotechnology, and medicine in obtaining novel bioactive compounds.

Potential topics include, but are not limited to, the following:

  • Whole-cell biocatalysis;
  • Lipase-catalyzed ester synthesis;
  • Enzymatic (trans)esterification;
  • Enzymatic synthesis of lipophilic antioxidants and antimicrobials;
  • Enzymatic lipophilization of phenolic extracts;
  • Lipid modification

Dr. Bartłomiej Zieniuk
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. Biomolecules 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

  • biocatalysis
  • biotransformation
  • enzyme-catalyzed reactions
  • whole-cell catalysis
  • green chemistry
  • enzymes
  • phenolic compounds
  • polyphenols
  • lipases
  • lipophilization
  • enzymatic synthesis
  • esterification
  • transesterification
  • green and sustainable chemistry approaches
  • lipid modification

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Further information on MDPI's Special Issue policies can be found here.

Published Papers (3 papers)

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Research

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14 pages, 5665 KiB  
Article
Sustainable Lipase Immobilization: Chokeberry and Apple Waste as Carriers
by Karina Jasińska, Maksym Nowosad, Aleksander Perzyna, Andrzej Bielacki, Stanisław Dziwiński, Bartłomiej Zieniuk and Agata Fabiszewska
Biomolecules 2024, 14(12), 1564; https://doi.org/10.3390/biom14121564 - 8 Dec 2024
Cited by 1 | Viewed by 958
Abstract
In the modern world, the principles of the bioeconomy are becoming increasingly important. Recycling and reusability play a crucial role in sustainable development. Green chemistry is based on enzymes, but immobilized biocatalysts are still often designed with synthetic polymers. Insoluble carriers for immobilized [...] Read more.
In the modern world, the principles of the bioeconomy are becoming increasingly important. Recycling and reusability play a crucial role in sustainable development. Green chemistry is based on enzymes, but immobilized biocatalysts are still often designed with synthetic polymers. Insoluble carriers for immobilized biocatalysts, particularly those derived from agro-industrial waste such as mesoporous lignocellulosic materials, offer a promising alternative. By using waste materials as support for enzymes, we can reduce the environmental impact of waste disposal and contribute to the development of efficient bioprocessing technologies. The current study aimed to assess the possibility of using apple and chokeberry pomace as carriers for the immobilization of Palatase 20000L (lipase from Rhizomucor miehei). The analysis of lignocellulosic materials revealed that chokeberry pomace has a higher neutral detergent fiber (NDF) and lignin contents than apple pomace. Moreover, Scanning Electron Microscopy (SEM) observations indicated similar compact structures in both pomaces. The lipase activity assays demonstrated that immobilization of lipase from R. miehei onto apple and chokeberry pomace improves their properties, especially the synthetic activity. The findings highlight the potential of utilizing fruit pomaces not only as a source of bioactive compounds but also in enhancing enzyme stability for industrial applications. Full article
(This article belongs to the Special Issue Recent Advances in the Enzymatic Synthesis of Bioactive Compounds)
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Review

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17 pages, 4127 KiB  
Review
Enzymatic Glycosylation of Ganoderma Terpenoid via Bacterial Glycosyltransferases and Glycoside Hydrolases
by Te-Sheng Chang, Jiumn-Yih Wu, Hsiou-Yu Ding and Tzi-Yuan Wang
Biomolecules 2025, 15(5), 655; https://doi.org/10.3390/biom15050655 - 1 May 2025
Viewed by 225
Abstract
Glycosylation is a critical enzymatic modification that involves the attachment of sugar moieties to target compounds, considerably influencing their physicochemical and biological characteristics. This review explored the role of two primary enzyme classes—glycosyltransferases (GTs) and glycoside hydrolases (GHs, glycosidases)—in catalyzing the glycosylation of [...] Read more.
Glycosylation is a critical enzymatic modification that involves the attachment of sugar moieties to target compounds, considerably influencing their physicochemical and biological characteristics. This review explored the role of two primary enzyme classes—glycosyltransferases (GTs) and glycoside hydrolases (GHs, glycosidases)—in catalyzing the glycosylation of natural products, with a specific focus on Ganoderma triterpenoids. While GTs typically use activated sugar donors, such as uridine diphosphate glucose, certain GHs can leverage more economical sugar sources, such as sucrose and starch, through transglycosylation. This paper also reviewed strategies for producing novel terpenoid glycosides, particularly recently isolated bacterial GTs and GHs capable of glycosylating terpenoids and flavonoids. It summarized the newly synthesized glycosides’ structures and biotransformation mechanisms, enhanced aqueous solubility, and potential applications. The regioselectivity and substrate specificity of GTs and GHs in catalyzing O-glycosylation (glucosylation) at distinct hydroxyl and carboxyl groups were compared. Furthermore, a special case in which the novel glycosylation reactions were mediated by GHs, including the formation of unique glycoside anomers, was included. The advantages and specific capabilities of GT/GH enzymes were evaluated for their potential in biotechnological applications and future research directions. Novel fungal triterpenoid glycosides produced through various glycosidases and sugars is expected to expand their potential applications in the future. Full article
(This article belongs to the Special Issue Recent Advances in the Enzymatic Synthesis of Bioactive Compounds)
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Other

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13 pages, 2356 KiB  
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A Refined Nomenclature System to Better Discriminate Endo- and Exo-Type Fructanases and Glucanases
by Laura Leaerts, Jaime Ricardo Porras-Domínguez, Maxime Versluys and Wim Van den Ende
Biomolecules 2025, 15(1), 11; https://doi.org/10.3390/biom15010011 - 25 Dec 2024
Cited by 2 | Viewed by 745
Abstract
Distinguishing between endo- and exo-type enzymes within the glycoside hydrolase (GH) classification presents significant challenges. Traditional methods, often based on endpoint activity measurements, do not capture the full range of products generated, leading to inconsistencies in classification. Not all exo-acting fructanases and glucanases [...] Read more.
Distinguishing between endo- and exo-type enzymes within the glycoside hydrolase (GH) classification presents significant challenges. Traditional methods, often based on endpoint activity measurements, do not capture the full range of products generated, leading to inconsistencies in classification. Not all exo-acting fructanases and glucanases produce monosaccharides (like fructose or glucose), while endo-acting enzymes do not solely produce higher-degree polymerization oligosaccharides. In practice, both enzyme types can yield a variety of products throughout the reaction, complicating classification efforts. To address these challenges, we propose a refined nomenclature system for GH enzymes, including fructanases and glucanases, based on good practices and initial product formation. This system classifies enzymes into four categories for each type: Fr, Fn, Fn,n+1 and F1 for fructanases, and Gr, Gn, Gn,n+1 and G1 for glucanases, based on their mode of action (endo- or exo-based) and initial product profiles. Our refined nomenclature system will advance enzyme structure–function research and support the production and application of fructan and glucan oligosaccharides as prebiotics, priming agents, and potential signaling molecules in microbe–microbe and plant–microbe interactions. Ultimately, this system could benefit agronomy and the food industry, contributing to health improvements. Full article
(This article belongs to the Special Issue Recent Advances in the Enzymatic Synthesis of Bioactive Compounds)
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