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Marine Drugs
Special Issues
Biotechnological Applications of Marine Enzymes
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Biotechnological Applications of Marine Enzymes

A special issue of Marine Drugs (ISSN 1660-3397). This special issue belongs to the section "Marine Biotechnology Related to Drug Discovery or Production".

Deadline for manuscript submissions: 31 July 2024 | Viewed by 4037

Special Issue Editors

Dr. Pasquale De Luca

E-Mail Website
Guest Editor
Research Infrastructure for Marine Biological Resources Department (RIMAR), Stazione Zoologica Anton Dohrn, 80121 Napoli, Italy
Interests: molecular biology; marine biotechnology; heterologous expression; enzymes; microalgae
Dr. Chiara Lauritano

E-Mail Website
Guest Editor
Stazione Zoologica Anton Dohrn, Villa Comunale, 80121 Naples, Italy
Interests: marine organisms, microalgae, transcriptomics, enzymes, bioactivity screening, genome-mining
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Due to the growing commercial demand for new and more efficient enzymes to implement and optimize industrial processes, many studies are now focusing their attention on new renewable and environmentally sustainable enzyme sources. This trend is also reflected in the increased number of publications in this area, especially in the use of marine microorganisms as sources of novel enzymes. With recent advances in omics technologies, there has been an increase in the amount of molecular data for in silico identification of enzymes and heterologous expression and successive production, shedding light on new enzymes of interest.

The aim of this Special Issue is to collect new and stimulating high-quality papers, including reviews and articles, directly related to various aspects of marine-derived enzymes and investigations into their possible applications.

Dr. Pasquale De Luca
Dr. Chiara Lauritano
Guest Editors

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. Marine Drugs 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 2900 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

  • enzymes
  • heterologous expression
  • marine organisms
  • omics technologies
  • genome mining
  • bioactivity screening
  • protein structure
  • biotechnological applications

Published Papers (2 papers)

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Research

19 pages, 2795 KiB  
Article
Bioinformatics-Based Screening Approach for the Identification and Characterization of Lipolytic Enzymes from the Marine Diatom Phaeodactylum tricornutum
by Victor Murison, Josiane Hérault, Benoît Schoefs, Justine Marchand and Lionel Ulmann
Mar. Drugs 2023, 21(2), 125; https://doi.org/10.3390/md21020125 - 14 Feb 2023
Cited by 2 | Viewed by 1803
Abstract
Oleaginous diatoms accumulate lipids of biotechnological interest when exposed to nutrient stress conditions such as nitrogen starvation. While accumulation mechanisms are well-known and have been engineered to improve lipid production, degradation mechanisms remain poorly investigated in diatoms. Identifying lipid-degrading enzymes is the initial [...] Read more.
Oleaginous diatoms accumulate lipids of biotechnological interest when exposed to nutrient stress conditions such as nitrogen starvation. While accumulation mechanisms are well-known and have been engineered to improve lipid production, degradation mechanisms remain poorly investigated in diatoms. Identifying lipid-degrading enzymes is the initial step to understanding the catabolic processes. In this study, an in silico screening of the genome of Phaeodactylum tricornutum led to the identification of 57 putative triacylglycerol lipases (EC 3.1.1.3) grouped in 4 families. Further analysis revealed the presence of conserved domains and catalytic residues of lipases. Physico-chemical characteristics and subcellular localization predictions highlighted that a majority of these putative proteins are hydrophilic and cytosolic, suggesting they could be recruited to lipid droplets directly from the cytosol. Among the 57 identified putative proteins, three lipases were identified as possibly involved in lipophagy due to a potential vacuolar localization. The expression of the mRNA corresponding to the 57 proteins was then searched in 3 transcriptomic datasets obtained under nitrogen starvation. Nine genes were highly regulated and were considered as encoding enzymes with a probable important function in lipid catabolism. A tertiary structure prediction of these nine candidates yielded eight functional 3D models. Among those, two downregulated enzymes, Phatr3_J54974 and Phatr3_EG00720, were highlighted as good targets for future functional genomics and purification studies to investigate their role in lipid degradation. Full article
(This article belongs to the Special Issue Biotechnological Applications of Marine Enzymes)
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12 pages, 2364 KiB  
Article
A Novel, Highly Potent NADPH-Dependent Cytochrome P450 Reductase from Waste Liza klunzingeri Liver
by Soudeh Bahramian Nasab, Ahmad Homaei, Roberto Fernandez-Lafuente, Jon Del Arco and Jesús Fernández-Lucas
Mar. Drugs 2023, 21(2), 99; https://doi.org/10.3390/md21020099 - 29 Jan 2023
Cited by 1 | Viewed by 1616
Abstract
The use of marine enzymes as catalysts for biotechnological applications is a topical subject. Marine enzymes usually display better operational properties than their animal, plant or bacterial counterparts, enlarging the range of possible biotechnological applications. Due to the fact that cytochrome P450 enzymes [...] Read more.
The use of marine enzymes as catalysts for biotechnological applications is a topical subject. Marine enzymes usually display better operational properties than their animal, plant or bacterial counterparts, enlarging the range of possible biotechnological applications. Due to the fact that cytochrome P450 enzymes can degrade many different toxic environmental compounds, these enzymes have emerged as valuable tools in bioremediation processes. The present work describes the isolation, purification and biochemical characterization of a liver NADPH-dependent cytochrome P450 reductase (CPR) from the marine fish Liza klunzingeri (LkCPR). Experimental results revealed that LkCPR is a monomer of approximately 75 kDa that is active in a wide range of pH values (6–9) and temperatures (40–60 °C), showing the highest catalytic activity at pH 8 and 50 °C. The activation energy of the enzyme reaction was 16.3 kcal mol−1 K−1. The KM values for cytochrome C and NADPH were 8.83 μM and 7.26 μM, and the kcat values were 206.79 s−1 and 202.93 s−1, respectively. LkCPR displayed a specific activity versus cytochrome C of 402.07 µmol min−1 mg1, the highest activity value described for a CPR up to date (3.2–4.7 times higher than the most active reported CPRs) and showed the highest thermostability described for a CPR. Taking into account all these remarkable catalytic features, LkCPR offers great potential to be used as a suitable biocatalyst. Full article
(This article belongs to the Special Issue Biotechnological Applications of Marine Enzymes)
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