Microbial Transformation of Organic Compounds

A special issue of Microorganisms (ISSN 2076-2607). This special issue belongs to the section "Microbial Biotechnology".

Deadline for manuscript submissions: closed (30 September 2023) | Viewed by 1588

Special Issue Editors


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Guest Editor
Institute of Biochemistry and Physiology of Microorganisms, Federal Research Center, Pushchino Scientific Center for Biological Research, Russian Academy of Sciences (FRC PSCBR RAS), Prospect Nauki 5, 142290 Pushchino, Russia
Interests: microbial biotechnology; steroid bioconversions; metabolic engineering; whole-cell catalysis
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Guest Editor
Laboratory of Microbial Transformation of Organic Compounds, Institute of Biochemistry and Physiology of Microorganisms (IBPM), 142290 Pushchino, Russia
Interests: biotransformation of steroids; biosynthesis of polypeptides
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The microbial transformation of organic compounds, i.e., the microbially catalyzed conversion of organic molecules, is a structural modification of the compounds by enzyme systems of microorganisms. It is a powerful tool to obtain organic molecules that are difficult to obtain by chemical means, which allows us to obtain compounds that are more active, and/or less toxic as compared with their parent molecules. As a rule, biotransformation is associated with the functionalization of the molecule, for example, by introducing oxygen-containing groups, while the basic structure of the molecule remains unchanged. This may result in the increase in the molecule’s polarity, solubility, affect the translocation throughout the membrane and influence the biological effects. Unlike chemical methods, microbial transformations can be carried out in aqueous media under mild conditions, which is especially important when working with unstable molecules subject to destruction in strongly alkaline or strongly acidic media, at high temperatures and pressure, under the influence of aggressive chemical agents that can be used in organic synthesis. Bioconversions can be carried out at molecule positions that cannot be achieved with chemical agents in a more regio- and stereospecific manner and usually do not require protection or deprotection of the functional groups. Metabolic pathways may be designed to increase biotransformation selectivity and suppress undesirable reactions. In this Special Issue of Microorganisms, we call for articles, reviews, short communications, or comments on different aspects of the microbial transformation of organic compounds, including (but not limited to) the following:

  • Antibiotics,
  • Antifungal agents,
  • Steroids,
  • Other medicines,
  • Xenobiotics and others.

Manuscripts related to the discovery and engineering of microorganisms capable of performing different reactions of oxyfunctionalization of inactive carbons, rare redox reactions, cascade reactions including (chemo)enzymatic cascades, detoxification of persistent organic pollutants through microbial transformation, creation and genetic modification of whole cell biocatalysts, application of immobilized cells, as well as the production of new and established value-added molecules via microbial synthesis or biotransformation are welcome.

Dr. Marina Donova
Dr. Victoria V. Fokina
Guest Editors

Manuscript Submission Information

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Keywords

  • microbial transformation
  • bioconversion
  • biocatalysis
  • microbial technology
  • metabolic engineering
  • protein engineering
  • bioactive compounds
  • bacteria
  • fungi

Published Papers (2 papers)

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Research

22 pages, 2011 KiB  
Article
Reconstruction of the Steroid 1(2)-Dehydrogenation System from Nocardioides simplex VKM Ac-2033D in Mycolicibacterium Hosts
by Svetlana R. Fufaeva, Dmitry V. Dovbnya, Tanya V. Ivashina, Andrei A. Shutov and Marina V. Donova
Microorganisms 2023, 11(11), 2720; https://doi.org/10.3390/microorganisms11112720 - 07 Nov 2023
Cited by 1 | Viewed by 731
Abstract
Microbial 1(2)-dehydrogenation of 3-ketosteroids is an important basis for the production of many steroid pharmaceuticals and synthons. When using the wild-type strains for whole cell catalysis, the undesirable reduction of the 20-carbonyl group, or 1(2)-hydrogenation, was observed. In this work, the recombinant strains [...] Read more.
Microbial 1(2)-dehydrogenation of 3-ketosteroids is an important basis for the production of many steroid pharmaceuticals and synthons. When using the wild-type strains for whole cell catalysis, the undesirable reduction of the 20-carbonyl group, or 1(2)-hydrogenation, was observed. In this work, the recombinant strains of Mycolicibacterium neoaurum and Mycolicibacterium smegmatis were constructed with blocked endogenous activity of 3-ketosteroid-9α-hydroxylase, 3-ketosteroid-1(2)-dehydrogenase (3-KSD), and expressing 3-KSD encoded by the gene KR76_27125 (kstD2NS) from Nocardioides simplex VKM Ac-2033D. The in vivo activity of the obtained recombinant strains against phytosterol, 6α-methyl-hydrocortisone, and hydrocortisone was studied. When using M. smegmatis as the host strain, the 1(2)-dehydrogenation activity of the constructed recombinant cells towards hydrocortisone was noticeably higher compared to those on the platform of M. neoaurum. A comparison of the strengths of inducible acetamidase and constitutive hsp60 promoters in M. smegmatis provided comparable results. Hydrocortisone biotransformation by M. smegmatis BD/pMhsp_k expressing kstD2NS resulted in 95.4% prednisolone yield, and the selectivity preferred that for N. simplex. Mycolicibacteria showed increased hydrocortisone degradation at 35 °C compared to 30 °C. The presence of endogenous steroid catabolism in Mycolicibacterium hosts does not seem to confer an advantage for the functioning of KstD2NS. The results allow for the evaluation of the prospects for the development of simple technological methods for the selective 1(2)-dehydrogenation of 3-ketosteroids by growing bacterial cells. Full article
(This article belongs to the Special Issue Microbial Transformation of Organic Compounds)
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25 pages, 8694 KiB  
Article
Unusual Oligomeric Laccase-like Oxidases from Ascomycete Curvularia geniculata VKM F-3561 Polymerizing Phenylpropanoids and Phenolic Compounds under Neutral Environmental Conditions
by Zhanna V. Renfeld, Alexey M. Chernykh, Boris P. Baskunov, Anastasya S. Gaidina, Nina M. Myasoedova, Anna D. Egorova, Olga V. Moiseeva, Sophya Yu Gorina and Marina P. Kolomytseva
Microorganisms 2023, 11(11), 2698; https://doi.org/10.3390/microorganisms11112698 - 03 Nov 2023
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Abstract
The unique oligomeric alkaliphilic laccase-like oxidases of the ascomycete C. geniculata VKM F-3561 (with molecular masses about 1035 and 870 kDa) were purified and characterized for the first time. The ability of the enzymes to oxidize phenylpropanoids and phenolic compounds under neutral environmental [...] Read more.
The unique oligomeric alkaliphilic laccase-like oxidases of the ascomycete C. geniculata VKM F-3561 (with molecular masses about 1035 and 870 kDa) were purified and characterized for the first time. The ability of the enzymes to oxidize phenylpropanoids and phenolic compounds under neutral environmental conditions with the formation of previously unknown di-, tri-, and tetrameric products of transformation was shown. The possibility to obtain industrially valuable compounds (dihydroxybenzyl alcohol and hydroxytyrosol) from caffeic acid using laccase-like oxidases of C. geniculata VKM F-3561 has been shown. Complete nucleotide sequence of the laccase gene, which is expressed at the peak of alkaliphilic laccase activity of the fungus, and its promoter region were determined. Based on the phylogenetic analysis of the nucleotide sequence, the nearest relationship of the isolated laccase gene with similar genes of fungi of the genera Alternaria, Bipolaris, and Cochliobolus was shown. Homologous model of the laccase structure was predicted and a proton channel was found, which was presumably responsible for the accumulation and transport of protons to T2/T3-copper center in the alkaliphilic laccase molecule and providing the functional activity of the enzyme in the neutral alkaline environment conditions. Full article
(This article belongs to the Special Issue Microbial Transformation of Organic Compounds)
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