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Journals
Microorganisms
Special Issues
Physiology and Enzymology of Hyper/Thermophiles
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Physiology and Enzymology of Hyper/Thermophiles

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

Deadline for manuscript submissions: closed (30 December 2023) | Viewed by 1066

Special Issue Editor

Dr. Kesen Ma

E-Mail Website
Guest Editor
Department of Biology, University of Waterloo, Waterloo, ON, Canada
Interests: enzymes; microbiology; biochemistry; enzymology; protein purification; protein analysis; hyperthermophiles
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Hyper/thermophiles have been isolated from various geothermal environments, including hot springs, volcanic areas, and deep-sea thermal vents. Many different types of hyper/thermophiles, such as heterotrophs, autotrophs, aerobes, and anaerobes, have been characterized, showing their diverse metabolic capabilities and physiological properties. Their remarkable features are high-temperature-dependent growth and heat-resistant macromolecules, especially for thermostable enzymes. Great progress has been made in understanding how proteins of hyper/thermophiles are stabilized, as well as in identifying their catalytic mechanisms and functions at high temperatures. Many thermostable enzymes from hyper/thermophiles have also been used in biotechnological applications. This Special Issue is dedicated to the topic of “Physiology and Enzymology of Hyper/thermophiles.”

Dr. Kesen Ma
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. Microorganisms 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

  • hyperthermophile
  • enzymology
  • physiology
  • metabolism
  • bio-catalysis
  • extremozyme
  • protein thermostability
  • growth at high temperature

Published Papers (1 paper)

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Research

13 pages, 3448 KiB  
Article
Molecular Characterization of the Iron-Containing Alcohol Dehydrogenase from the Extremely Thermophilic Bacterium Pseudothermotoga hypogea
by Liangliang Hao, Zainab Ayinla and Kesen Ma
Microorganisms 2024, 12(2), 311; https://doi.org/10.3390/microorganisms12020311 - 1 Feb 2024
Viewed by 775
Abstract
Pseudothermotoga hypogea is an extremely thermophilic bacterium capable of growing at 90 °C and producing ethanol, which is catalyzed by an alcohol dehydrogenase (ADH). The gene encoding P. hypogea ADH (PhADH) was cloned, sequenced and over-expressed. The gene sequence (1164 bp) [...] Read more.
Pseudothermotoga hypogea is an extremely thermophilic bacterium capable of growing at 90 °C and producing ethanol, which is catalyzed by an alcohol dehydrogenase (ADH). The gene encoding P. hypogea ADH (PhADH) was cloned, sequenced and over-expressed. The gene sequence (1164 bp) was obtained by sequencing all fragments of the gene, which were amplified from the genomic DNA. The deduced amino acid sequence showed high identity to iron-containing ADHs from other Thermotoga species and harbored typical iron- and NADP-binding motifs, Asp195His199His268His282 and Gly39Gly40Gly41Ser42, respectively. Structural modeling showed that the N-terminal domain of PhADH contains an α/β-dinucleotide-binding motif and that its C-terminal domain is an α-helix-rich region containing the iron-binding motif. The recombinant PhADH was soluble, active, and thermostable, with a subunit size of 43 ± 1 kDa revealed by SDS-PAGE analyses. The recombinant PhADH (69 ± 2 U/mg) was shown to have similar properties to the native enzyme. The optimal pH values for alcohol oxidation and aldehyde reduction were 11.0 and 8.0, respectively. It was also thermostable, with a half-life of 5 h at 70 °C. The successful expression of the recombinant PhADH in E. coli significantly enhanced the yield of enzyme production and thus will facilitate further investigation of the catalytic mechanisms of iron-containing ADHs. Full article
(This article belongs to the Special Issue Physiology and Enzymology of Hyper/Thermophiles)
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