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Biocatalysis and Bioactive Molecules: Future and Development
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Biocatalysis and Bioactive Molecules: Future and Development

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 20 April 2025 | Viewed by 11477

Special Issue Editor

Dr. Lindomar Alberto Lerin

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Guest Editor
Department of Chemistry, Pharmaceutical and Agricultural Sciences, University of Ferrara, Via Luigi Borsari, 46, 44121 Ferrara, Italy
Interests: biocatalysis; enzyme; lipases; enzymatic synthesis; bioprocess optimization; bio-compounds synthesis; bioreactor; continuous mode; batch; fed-batch; solvent-free reactions; bioactive biomolecules; renewable sources; biotechnological processes; green chemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Biocatalysis has increasingly been used for synthesising compounds to make manufacturing processes greener and more sustainable. In addition, different industry sectors either already use or show increasing interest in molecules obtained via bioprocesses because they are products with high added value and are recognised as natural. Bioactive molecules produced biocatalytically can improve the quality of life, having beneficial impacts on the health of the human body in the prevention and treatment of various chronic diseases, and are environmentally friendly. However, improving existing techniques and developing new methodologies are necessary to increase their synthesis. Furthermore, studies of strategies to reduce economic impacts have received attention, such as the search for new enzymes, new supports for enzyme immobilisation, biocatalysts reuse, reactor configuration, process optimisation and use of alternative substrates, mainly agro-industrial waste, and these must be evaluated. This research topic encourages article publication related to enzyme production and immobilisation and enzymatic synthesis, mainly through valuing renewable resources, with an interest in the cosmetic, pharmaceutical, nutraceutical and food industries. Herewith, the development and trends of biocatalysis for active biomolecules producing industrial interest are highlighted.

We invite investigators to contribute original research, reviews and perspective articles that address the progress and current knowledge of the biosynthesis and characterisation of bioactive molecules, biocatalysis processes, processes with enzymatic routes, enzyme immobilisation and new supports for enzyme immobilisation, new biomolecules synthesis, green processes and technologies, new bioprocess design, bioconversion of agro-industrial waste and circular bio-based economy. We are also more than honored to announce that Dr. Daniela Remonatto (from São Paulo State University, Brazil) will participate in this Special Issue.

Dr. Lindomar Alberto Lerin
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

  • enzymatic synthesis
  • renewable sources
  • biocatalysis
  • enzymes
  • bioactive molecules
  • green chemistry
  • bioprocess
  • green catalysis
  • biotechnology
  • agro-industrial waste
  • immobilization
  • green solvent

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Published Papers (6 papers)

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Editorial

Jump to: Research, Review

2 pages, 171 KiB  
Editorial
Biocatalysis and Bioactive Molecules: Future and Development
by Daniela Remonatto and Lindomar Alberto Lerin
Int. J. Mol. Sci. 2023, 24(6), 5571; https://doi.org/10.3390/ijms24065571 - 14 Mar 2023
Cited by 5 | Viewed by 1404
Abstract
Due to the increasing interest in molecules obtained by bioprocesses over the past decade, biocatalysis has gained momentum in a variety of industrial sectors [...] Full article
(This article belongs to the Special Issue Biocatalysis and Bioactive Molecules: Future and Development)

Research

Jump to: Editorial, Review

21 pages, 3582 KiB  
Article
Antimicrobial Activity of Chalcones with a Chlorine Atom and Their Glycosides
by Agnieszka Krawczyk-Łebek, Barbara Żarowska, Tomasz Janeczko and Edyta Kostrzewa-Susłow
Int. J. Mol. Sci. 2024, 25(17), 9718; https://doi.org/10.3390/ijms25179718 - 8 Sep 2024
Viewed by 712
Abstract
Chalcones, secondary plant metabolites, exhibit various biological properties. The introduction of a chlorine and a glucosyl substituent to the chalcone could enhance its bioactivity and bioavailability. Such compounds can be obtained through a combination of chemical and biotechnological methods. Therefore, 4-chloro-2′-hydroxychalcone and 5′-chloro-2′-hydroxychalcone [...] Read more.
Chalcones, secondary plant metabolites, exhibit various biological properties. The introduction of a chlorine and a glucosyl substituent to the chalcone could enhance its bioactivity and bioavailability. Such compounds can be obtained through a combination of chemical and biotechnological methods. Therefore, 4-chloro-2′-hydroxychalcone and 5′-chloro-2′-hydroxychalcone were obtained by synthesis and then glycosylated in two filamentous fungi strains cultures, i.e., Isaria fumosorosea KCH J2 and Beauveria bassiana KCH J1.5. The main site of the glycosylation of both compounds by I. fumosorosea KCH J2 was C-2′ and C-3 when the second strain was utilized. The pharmacokinetics of these compounds were predicted using chemoinformatics tools. Furthermore, antimicrobial activity tests were performed. Compounds significantly inhibited the growth of the bacteria strains Escherichia coli 10536, Staphylococcus aureus DSM 799, and yeast Candida albicans DSM 1386. Nevertheless, the bacterial strain Pseudomonas aeruginosa DSM 939 exhibited significant resistance to their effects. The growth of lactic acid bacteria strain Lactococcus acidophilus KBiMZ 01 bacteria was moderately inhibited, but strains Lactococcus rhamnosus GG and Streptococcus thermophilus KBM-1 were completely inhibited. In summary, chalcones substituted with a chlorine demonstrated greater efficacy in inhibiting the microbial strains under examination compared to 2′-hydroxychalcone, while aglycones and their glycosides exhibited similar effectiveness. Full article
(This article belongs to the Special Issue Biocatalysis and Bioactive Molecules: Future and Development)
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17 pages, 2392 KiB  
Article
Optimizing the First Step of the Biocatalytic Process for Green Leaf Volatiles Production: Lipase-Catalyzed Hydrolysis of Three Vegetable Oils
by Eva Faillace, Virginie Brunini-Bronzini de Caraffa, Magali Mariani, Liliane Berti, Jacques Maury and Sophie Vincenti
Int. J. Mol. Sci. 2023, 24(15), 12274; https://doi.org/10.3390/ijms241512274 - 31 Jul 2023
Cited by 1 | Viewed by 1256
Abstract
Green leaf volatiles (GLVs), including short chain volatile aldehydes, are widely used in the flavor and food industries because of their fresh aroma. To meet the growing demand for natural GLVs with high added value, the use of biocatalytic processes appears as a [...] Read more.
Green leaf volatiles (GLVs), including short chain volatile aldehydes, are widely used in the flavor and food industries because of their fresh aroma. To meet the growing demand for natural GLVs with high added value, the use of biocatalytic processes appears as a relevant application. In such processes, vegetable oils are bioconverted into GLVs. First, the triacylglycerols of the oils are hydrolyzed by a lipase. Then, the free polyunsaturated fatty acids are converted by a lipoxygenase. Finally, volatile C6 or C9 aldehydes and 9- or 12-oxoacids are produced with a hydroperoxide lyase. Optimization of each biocatalytic step must be achieved to consider a scale-up. In this study, three oils (sunflower, hempseed, and linseed oils) and three lipases (Candida rugosa, Pseudomonas fluorescens, and Rhizomucor miehei lipases) have been tested to optimize the first step of the process. The experimental design and response surface methodology (RSM) were used to determine the optimal hydrolysis conditions for each oil. Five factors were considered, i.e., pH, temperature, reaction duration, enzyme load, and oil/aqueous ratio of the reaction mixture. Candida rugosa lipase was selected as the most efficient enzyme to achieve conversion of 96 ± 1.7%, 97.2 ± 3.8%, and 91.8 ± 3.2%, respectively, for sunflower, hempseed, and linseed oils under the defined optimized reaction conditions. Full article
(This article belongs to the Special Issue Biocatalysis and Bioactive Molecules: Future and Development)
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14 pages, 6483 KiB  
Article
A New Hypoglycemic Prenylated Indole Alkaloid N-Oxide from Endophytic Fungus Pallidocercospora crystalline
by Shuo Gao, Xiao Lin, Yeqin Shi, Hu Zhou, Xiao Zheng, Mingyu Li and Ting Lin
Int. J. Mol. Sci. 2023, 24(10), 8767; https://doi.org/10.3390/ijms24108767 - 15 May 2023
Viewed by 1506
Abstract
A new prenylated indole alkaloid—Penicimutamide C N-oxide (1), a new alkaloid penicimutamine A (2), along with six known alkaloids were isolated from an endophytic fungus Pallidocercospora crystallina. A simple and accurate method was used to determine the [...] Read more.
A new prenylated indole alkaloid—Penicimutamide C N-oxide (1), a new alkaloid penicimutamine A (2), along with six known alkaloids were isolated from an endophytic fungus Pallidocercospora crystallina. A simple and accurate method was used to determine the N-O bond in the N-oxide group of 1. By using a β-cell ablation diabetic zebrafish model, compounds 1, 3, 5, 6 and 8 showed significantly hypoglycemic activities under the concentration of 10 μM. Further studies revealed that compounds 1 and 8 lowered the glucose level through promoting glucose uptake in zebrafish. In addition, all eight compounds showed no acute toxicity, teratogenicity, nor vascular toxicity in zebrafish under the concentrations range from 2.5 μΜ to 40 μM. Importantly, these results provide new lead compounds for the development of antidiabetes strategies. Full article
(This article belongs to the Special Issue Biocatalysis and Bioactive Molecules: Future and Development)
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14 pages, 3217 KiB  
Communication
Synthesis and Characterization of Aminoamidine-Based Polyacrylonitrile Fibers for Lipase Immobilization with Effective Reusability and Storage Stability
by Yasser M. Al Angari, Yaaser Q. Almulaiky, Maha M. Alotaibi, Mahmoud A. Hussein and Reda M. El-Shishtawy
Int. J. Mol. Sci. 2023, 24(3), 1970; https://doi.org/10.3390/ijms24031970 - 19 Jan 2023
Cited by 11 | Viewed by 1720
Abstract
Lipases are extensively utilized industrial biocatalysts that play an important role in various industrial and biotechnological applications. Herein, polyacrylonitrile (PAN) was treated with hexamethylene diamine (HMDA) and activated by glutaraldehyde, then utilized as a carrier support for Candida rugosa lipase. In this regard, [...] Read more.
Lipases are extensively utilized industrial biocatalysts that play an important role in various industrial and biotechnological applications. Herein, polyacrylonitrile (PAN) was treated with hexamethylene diamine (HMDA) and activated by glutaraldehyde, then utilized as a carrier support for Candida rugosa lipase. In this regard, the morphological structure of modified PAN before and after the immobilization process was evaluated using FTIR and SEM analyses. The immobilized lipase exhibited the highest activity at pH 8.0, with an immobilization yield of 81% and an activity of 91%. The optimal pH and temperature for free lipase were 7.5 and 40 °C, while the immobilized lipase exhibited its optimal activity at a pH of 8.0 and a temperature of 50 °C. After recycling 10 times, the immobilized lipase maintained 76% of its activity and, after 15 reuses, it preserved 61% of its activity. The lipase stability was significantly improved after immobilization, as it maintained 76% of its initial activity after 60 days of storage. The calculated Km values were 4.07 and 6.16 mM for free and immobilized lipase, and the Vmax values were 74 and 77 μmol/mL/min, respectively. These results demonstrated that synthetically modified PAN is appropriate for immobilizing enzymes and has the potential for commercial applications. Full article
(This article belongs to the Special Issue Biocatalysis and Bioactive Molecules: Future and Development)
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Review

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27 pages, 23801 KiB  
Review
Epoxide Hydrolases: Multipotential Biocatalysts
by Marek Bučko, Katarína Kaniaková, Helena Hronská, Peter Gemeiner and Michal Rosenberg
Int. J. Mol. Sci. 2023, 24(8), 7334; https://doi.org/10.3390/ijms24087334 - 15 Apr 2023
Cited by 15 | Viewed by 3477
Abstract
Epoxide hydrolases are attractive and industrially important biocatalysts. They can catalyze the enantioselective hydrolysis of epoxides to the corresponding diols as chiral building blocks for bioactive compounds and drugs. In this review article, we discuss the state of the art and development potential [...] Read more.
Epoxide hydrolases are attractive and industrially important biocatalysts. They can catalyze the enantioselective hydrolysis of epoxides to the corresponding diols as chiral building blocks for bioactive compounds and drugs. In this review article, we discuss the state of the art and development potential of epoxide hydrolases as biocatalysts based on the most recent approaches and techniques. The review covers new approaches to discover epoxide hydrolases using genome mining and enzyme metagenomics, as well as improving enzyme activity, enantioselectivity, enantioconvergence, and thermostability by directed evolution and a rational design. Further improvements in operational and storage stabilization, reusability, pH stabilization, and thermal stabilization by immobilization techniques are discussed in this study. New possibilities for expanding the synthetic capabilities of epoxide hydrolases by their involvement in non-natural enzyme cascade reactions are described. Full article
(This article belongs to the Special Issue Biocatalysis and Bioactive Molecules: Future and Development)
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