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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: 15 January 2025 | Viewed by 11554

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
Interests: microalgae; drug discovery; gene mining; marine biotechnology; transcriptomics
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

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Published Papers (6 papers)

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Research

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21 pages, 7837 KiB  
Article
Salinity Stress Acclimation Strategies in Chlamydomonas sp. Revealed by Physiological, Morphological and Transcriptomic Approaches
by Chiara Lauritano, Emma Bazzani, Eleonora Montuori, Francesco Bolinesi, Olga Mangoni, Gennaro Riccio, Angela Buondonno and Maria Saggiomo
Mar. Drugs 2024, 22(8), 351; https://doi.org/10.3390/md22080351 - 29 Jul 2024
Viewed by 978
Abstract
Climate changes may include variations in salinity concentrations at sea by changing ocean dynamics. These variations may be especially challenging for marine photosynthetic organisms, affecting their growth and distribution. Chlamydomonas spp. are ubiquitous and are often found in extreme salinity conditions. For this [...] Read more.
Climate changes may include variations in salinity concentrations at sea by changing ocean dynamics. These variations may be especially challenging for marine photosynthetic organisms, affecting their growth and distribution. Chlamydomonas spp. are ubiquitous and are often found in extreme salinity conditions. For this reason, they are considered good model species to study salinity adaptation strategies. In the current study, we used an integrated approach to study the Chlamydomonas sp. CCMP225 response to salinities of 20‰ and 70‰, by combining physiological, morphological, and transcriptomic analyses, and comparing differentially expressed genes in the exponential and stationary growth phases under the two salinity conditions. The results showed that the strain is able to grow under all tested salinity conditions and maintains a surprisingly high photosynthetic efficiency even under high salinities. However, at the highest salinity condition, the cells lose their flagella. The transcriptomic analysis highlighted the up- or down-regulation of specific gene categories, helping to identify key genes responding to salinity stress. Overall, the findings may be of interest to the marine biology, ecology, and biotechnology communities, to better understand species adaptation mechanisms under possible global change scenarios and the potential activation of enzymes involved in the synthesis of bioactive molecules. Full article
(This article belongs to the Special Issue Biotechnological Applications of Marine Enzymes)
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18 pages, 2645 KiB  
Article
Potential of Marine Bacterial Metalloprotease A69 in the Preparation of Peanut Peptides with Angiotensin-Converting Enzyme (ACE)-Inhibitory and Antioxidant Properties
by Wen-Jie Cao, Rui Liu, Wen-Xiao Zhao, Jian Li, Yan Wang, Xiao-Jie Yuan, Hui-Lin Wang, Yu-Zhong Zhang, Xiu-Lan Chen and Yu-Qiang Zhang
Mar. Drugs 2024, 22(7), 305; https://doi.org/10.3390/md22070305 - 29 Jun 2024
Viewed by 996
Abstract
Marine bacterial proteases have rarely been used to produce bioactive peptides, although many have been reported. This study aims to evaluate the potential of the marine bacterial metalloprotease A69 from recombinant Bacillus subtilis in the preparation of peanut peptides (PPs) with antioxidant activity [...] Read more.
Marine bacterial proteases have rarely been used to produce bioactive peptides, although many have been reported. This study aims to evaluate the potential of the marine bacterial metalloprotease A69 from recombinant Bacillus subtilis in the preparation of peanut peptides (PPs) with antioxidant activity and angiotensin-converting enzyme (ACE)-inhibitory activity. Based on the optimization of the hydrolysis parameters of protease A69, a process for PPs preparation was set up in which the peanut protein was hydrolyzed by A69 at 3000 U g−1 and 60 °C, pH 7.0 for 4 h. The prepared PPs exhibited a high content of peptides with molecular weights lower than 1000 Da (>80%) and 3000 Da (>95%) and contained 17 kinds of amino acids. Moreover, the PPs displayed elevated scavenging of hydroxyl radical and 1,1-diphenyl-2-picryl-hydrazyl radical, with IC50 values of 1.50 mg mL−1 and 1.66 mg mL−1, respectively, indicating the good antioxidant activity of the PPs. The PPs also showed remarkable ACE-inhibitory activity, with an IC50 value of 0.71 mg mL−1. By liquid chromatography mass spectrometry analysis, the sequences of 19 ACE inhibitory peptides and 15 antioxidant peptides were identified from the PPs. These results indicate that the prepared PPs have a good nutritional value, as well as good antioxidant and antihypertensive effects, and that the marine bacterial metalloprotease A69 has promising potential in relation to the preparation of bioactive peptides from peanut protein. Full article
(This article belongs to the Special Issue Biotechnological Applications of Marine Enzymes)
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11 pages, 2271 KiB  
Article
A Hadal Streptomyces-Derived Echinocandin Acylase Discovered through the Prioritization of Protein Families
by Xuejian Jiang, Hongjun Shu, Shuting Feng, Pinmei Wang, Zhizhen Zhang and Nan Wang
Mar. Drugs 2024, 22(5), 212; https://doi.org/10.3390/md22050212 - 7 May 2024
Viewed by 1191
Abstract
Naturally occurring echinocandin B and FR901379 are potent antifungal lipopeptides featuring a cyclic hexapeptide nucleus and a fatty acid side chain. They are the parent compounds of echinocandin drugs for the treatment of severe fungal infections caused by the Candida and Aspergilla species. [...] Read more.
Naturally occurring echinocandin B and FR901379 are potent antifungal lipopeptides featuring a cyclic hexapeptide nucleus and a fatty acid side chain. They are the parent compounds of echinocandin drugs for the treatment of severe fungal infections caused by the Candida and Aspergilla species. To minimize hemolytic toxicity, the native fatty acid side chains in these drug molecules are replaced with designer acyl side chains. The deacylation of the N-acyl side chain is, therefore, a crucial step for the development and manufacturing of echinocandin-type antibiotics. Echinocandin E (ECE) is a novel echinocandin congener with enhanced stability generated via the engineering of the biosynthetic machinery of echinocandin B (ECB). In the present study, we report the discovery of the first echinocandin E acylase (ECEA) using the enzyme similarity tool (EST) for enzymatic function mining across protein families. ECEA is derived from Streptomyces sp. SY1965 isolated from a sediment collected from the Mariana Trench. It was cloned and heterologously expressed in S. lividans TK24. The resultant TKecea66 strain showed efficient cleavage activity of the acyl side chain of ECE, showing promising applications in the development of novel echinocandin-type therapeutics. Our results also provide a showcase for harnessing the essentially untapped biodiversity from the hadal ecosystems for the discovery of functional molecules. Full article
(This article belongs to the Special Issue Biotechnological Applications of Marine Enzymes)
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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 4 | Viewed by 2261
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 1985
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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Review

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17 pages, 988 KiB  
Review
Marine-Derived Lipases for Enhancing Enrichment of Very-Long-Chain Polyunsaturated Fatty Acids with Reference to Omega-3 Fatty Acids
by Mahejbin Karia, Mona Kaspal, Mariam Alhattab and Munish Puri
Mar. Drugs 2024, 22(7), 301; https://doi.org/10.3390/md22070301 - 28 Jun 2024
Viewed by 3206
Abstract
Omega-3 fatty acids are essential fatty acids that are not synthesised by the human body and have been linked with the prevention of chronic illnesses such as cardiovascular and neurodegenerative diseases. However, the current dietary habits of the majority of the population include [...] Read more.
Omega-3 fatty acids are essential fatty acids that are not synthesised by the human body and have been linked with the prevention of chronic illnesses such as cardiovascular and neurodegenerative diseases. However, the current dietary habits of the majority of the population include lower omega-3 content compared to omega-6, which does not promote good health. To overcome this, pharmaceutical and nutraceutical companies aim to produce omega-3-fortified foods. For this purpose, various approaches have been employed to obtain omega-3 concentrates from sources such as fish and algal oil with higher amounts of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA). Among these techniques, enzymatic enrichment using lipase enzymes has gained tremendous interest as it is low in capital cost and simple in operation. Microorganism-derived lipases are preferred as they are easily produced due to their higher growth rate, and they hold the ability to be manipulated using genetic modification. This review aims to highlight the recent studies that have been carried out using marine lipases for the enrichment of omega-3, to provide insight into future directions. Overall, the covalent bond-based lipase immobilization to various support materials appears most promising; however, greener and less expensive options need to be strengthened. Full article
(This article belongs to the Special Issue Biotechnological Applications of Marine Enzymes)
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