Cold-Adapted Bacteria and Marine Bacteria

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

Deadline for manuscript submissions: closed (31 December 2024) | Viewed by 2788

Special Issue Editor


E-Mail Website
Guest Editor
Dipartimento di Scienze Chimiche, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cintia 4, 80126 Napoli, Italy
Interests: Pseudoalteromonas haloplanktis genetics and genomics; psychrophilic bacteria fermentation; psychrophilic bacteria physiology; bioactive compounds from marine bacteria; recombinant protein production in Pseudoalteromonas haloplanktis
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue is the continuation of our previous Special Issue, entitled "Biotechnology of Cold-Adapted Bacteria and Marine Bacteria", which was published in 2021:

Permanent or transient cold environments are prevalent on our planet. Indeed, besides the polar and alpine areas, a large portion of seawater has a temperature below 15 °C. We are approaching the study of the microbiome that thrives in these habitats, uncovering a “world of opportunities” for biotechnologists.

This Special Issue aims to report the cutting-edge applications of microorganisms isolated from sea and/or from cold environments, their enzymes, and their chemical diversity in different fields of modern biotechnologies, such as (and not limited to) the following:

  • Food applications;
  • Detergents and the cleaning industry;
  • Environmental biotechnologies (wastewater treatments and bioremediation);
  • Biofuels and energy production;
  • Molecular as well as structural biology and recombinant protein production;
  • Pharmaceutical and medical industry.

Dr. Maria Luisa Tutino
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

  • cold-adapted enzyme
  • cold-adapted bacteria
  • marine bacteria
  • white biotechnologies
  • enzyme catalysis
  • microbial catalysis
  • food biotechnologies
  • environmental biotechnologies
  • detergent industry
  • cleaning industry
  • biofuels
  • molecular biology
  • recombinant protein production
  • pharmaceutical industry
  • structural biology

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • e-Book format: Special Issues with more than 10 articles can be published as dedicated e-books, ensuring wide and rapid dissemination.

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

Published Papers (3 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

24 pages, 2047 KiB  
Article
Engineering the Marine Pseudoalteromonas haloplanktis TAC125 via the pMEGA Plasmid Targeted Curing Using PTasRNA Technology
by Angelica Severino, Concetta Lauro, Marzia Calvanese, Christopher Riccardi, Andrea Colarusso, Marco Fondi, Ermenegilda Parrilli and Maria Luisa Tutino
Microorganisms 2025, 13(2), 324; https://doi.org/10.3390/microorganisms13020324 - 2 Feb 2025
Viewed by 290
Abstract
Marine bacteria that have adapted to thrive in extreme environments, such as Pseudoalteromonas haloplanktis TAC125 (PhTAC125), offer a unique biotechnological potential. The discovery of an endogenous megaplasmid (pMEGA) raises questions about its metabolic impact and functional role in that strain. This [...] Read more.
Marine bacteria that have adapted to thrive in extreme environments, such as Pseudoalteromonas haloplanktis TAC125 (PhTAC125), offer a unique biotechnological potential. The discovery of an endogenous megaplasmid (pMEGA) raises questions about its metabolic impact and functional role in that strain. This study aimed at streamlining the host genetic background by curing PhTAC125 of the pMEGA plasmid using a sequential genetic approach. We combined homologous recombination by exploiting a suicide vector, with the PTasRNA gene-silencing technology interfering with pMEGA replication machinery. This approach led to the construction of the novel PhTAC125 KrPL2 strain, cured of the pMEGA plasmid, which exhibited no significant differences in growth behavior, though showcasing enhanced resistance to oxidative stress and a reduced capacity for biofilm formation. These findings represent a significant achievement in developing our understanding of the role of the pMEGA plasmid and the biotechnological applications of PhTAC125 in recombinant protein production. This opens up the possibility of exploiting valuable pMEGA genetic elements and further advancing the genetic tools for PhTAC125. Full article
(This article belongs to the Special Issue Cold-Adapted Bacteria and Marine Bacteria)
Show Figures

Figure 1

20 pages, 1914 KiB  
Article
Production, Purification, and Biochemical Characterization of a Novel ATP-Dependent Caseinolytic Protease from the Marine Bacterium Cobetia amphilecti KMM 296
by Yulia Noskova, Olga Nedashkovskaya and Larissa Balabanova
Microorganisms 2025, 13(2), 307; https://doi.org/10.3390/microorganisms13020307 - 30 Jan 2025
Viewed by 305
Abstract
A novel caseinolytic protease (ClpP) of the S14 family from Cobetia amphilecti KMM 296 (CamClpP), comprising 206 amino acids, with a calculated molecular weight of 22.66 kDa and a pI of 4.88, was expressed in Escherichia coli cells to verify the functional annotation [...] Read more.
A novel caseinolytic protease (ClpP) of the S14 family from Cobetia amphilecti KMM 296 (CamClpP), comprising 206 amino acids, with a calculated molecular weight of 22.66 kDa and a pI of 4.88, was expressed in Escherichia coli cells to verify the functional annotation of the encoding gene that has low identity with known structures. The proteolytic activity of the purified recombinant enzyme was found to be 2824 U/mg, using 1% casein as a substrate. Enzyme activity was maximal at pH 5.6 and 7.4 in phosphate buffer and was maintained over a wide pH range of 4-10. The optimum temperature for protease activity was 45 °C. The enzyme in its optimal state required the presence of either NaCl or KCl at concentrations of 0.3 and 0.2 M, respectively. The addition of the metal ions Mg2+, Ca2+, Ni2+, Mn2+, Li+, and Zn2+ at 2 mM resulted in a significant inhibition of the protease activity. However, the presence of Co2+ led to a marked activation of the enzyme in the absence of ATP. The enzyme activity was inhibited by ethanol, isopropanol, glycerol, SDS, EGTA, and EDTA. The presence of Triton X-100, acetone, DTT, and PMSF resulted in a significant increase in the CamClpP protease activity. The protease CamClpP effectively and preferentially degrades high-polymer wheat and rye flour proteins. This new proteolytic enzyme with unique properties is of great ecological and biotechnological importance. Full article
(This article belongs to the Special Issue Cold-Adapted Bacteria and Marine Bacteria)
12 pages, 2173 KiB  
Article
Exploring the Frozen Armory: Antiphage Defense Systems in Cold-Adapted Bacteria with a Focus on CRISPR-Cas Systems
by Greta Daae Sandsdalen, Animesh Kumar and Erik Hjerde
Microorganisms 2024, 12(5), 1028; https://doi.org/10.3390/microorganisms12051028 - 20 May 2024
Viewed by 1800
Abstract
Our understanding of the antiphage defense system arsenal in bacteria is rapidly expanding, but little is known about its occurrence in cold-adapted bacteria. In this study, we aim to shed light on the prevalence and distribution of antiphage defense systems in cold-adapted bacteria, [...] Read more.
Our understanding of the antiphage defense system arsenal in bacteria is rapidly expanding, but little is known about its occurrence in cold-adapted bacteria. In this study, we aim to shed light on the prevalence and distribution of antiphage defense systems in cold-adapted bacteria, with a focus on CRISPR-Cas systems. Using bioinformatics tools, Prokaryotic Antiviral Defense LOCator (PADLOC) and CRISPRCasTyper, we mapped the presence and diversity of antiphage defense systems in 938 available genomes of cold-adapted bacteria from diverse habitats. We confirmed that CRISPR-Cas systems are less frequent in cold-adapted bacteria, compared to mesophilic and thermophilic species. In contrast, several antiphage defense systems, such as dXTPases and DRTs, appear to be more frequently compared to temperate bacteria. Additionally, our study provides Cas endonuclease candidates with a potential for further development into cold-active CRISPR-Cas genome editing tools. These candidates could have broad applications in research on cold-adapted organisms. Our study provides a first-time map of antiphage defense systems in cold-adapted bacteria and a detailed overview of CRISPR-Cas diversity. Full article
(This article belongs to the Special Issue Cold-Adapted Bacteria and Marine Bacteria)
Show Figures

Figure 1

Back to TopTop