Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
9.6
4.9
Journals
Marine Drugs
Special Issues
Advances of Marine-Derived Enzymes
share announcement

Advances of Marine-Derived 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 May 2025 | Viewed by 10137

Special Issue Editor

Dr. Olafur Fridjonsson

E-Mail Website
Guest Editor
Matís Ohf., Reykjavik, Iceland
Interests: biotechnology; genome/metagenome analysis; marine enzymes; marine polysaccharides; bioactive compounds
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,                

Marine enzymes are different from terrestrial enzymes in many ways. They have evolved specificity and affinity for marine molecules, which are often recalcitrant to terrestrial enzymes. The diverse and complex marine environments with high salinity, high pressure, low temperature, and special lighting conditions have also contributed to their specific features. In recent years, interest in marine biotechnology has increased. Marine biomass, such as seaweed, can be considered a preferable alternative to terrestrial plants for refining nutrients, bioenergy compounds, bioactive molecules, and other chemicals, as the latter feedstock is reliant on water, land, fertilizers, and pesticides, and also competes with crops that are intended for human consumption. The enzymatic refining of marine feedstock such as seaweed to added value products is, however, still rare to find on an industrial scale. There is a need for suitable and advantageous enzymatic tools. The bioprospecting of marine enzymes with industrial application potentials is therefore still of great interest.

A Special Issue on advances in marine derived enzymes is now planned for publication in the journal Marine Drugs. The focus will be on enzymes from both marine microbial and multicellular organisms. New marine enzymes, enzyme products, properties, and production technology, as well as exploitation potential in marine biotechnology will be highlighted.

Dr. Olafur Fridjonsson
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. 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

  • marine enzymes
  • enzyme products
  • enzyme properties
  • exploitation potentials
  • marine biotechnology
  • biorefining
  • production technology

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 policies can be found here.

Published Papers (8 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

15 pages, 5117 KiB  
Article
Heterologous Expression and Biochemical Characterization of a New α-Amylase from Nocardiopsis aegyptia HDN19-252 of Antarctic Animal Origin
by Fuhao Liu, Xiangnan Zheng, Wenhui Liao, Xingtao Ren, Chuanteng Ma, Guojian Zhang, Qian Che, Tianjiao Zhu, Wenxue Wang, Tao Zhang, Feng Han and Dehai Li
Mar. Drugs 2025, 23(4), 159; https://doi.org/10.3390/md23040159 - 4 Apr 2025
Viewed by 487
Abstract
α-Amylases, catalyzing starch degradation, serve as vital biocatalysts in industrial and pharmaceutical applications. This study identified a new α-amylase, Alphaz, from Nocardiopsis aegyptia HDN19-252 of Antarctic animal origin, achieving heterologous expression in Escherichia coli. Phylogenetic analysis confirmed its classification into the GH13_5 [...] Read more.
α-Amylases, catalyzing starch degradation, serve as vital biocatalysts in industrial and pharmaceutical applications. This study identified a new α-amylase, Alphaz, from Nocardiopsis aegyptia HDN19-252 of Antarctic animal origin, achieving heterologous expression in Escherichia coli. Phylogenetic analysis confirmed its classification into the GH13_5 subfamily of glycoside hydrolases. Recombinant Alphaz exhibited optimal activity at 40 °C/pH 8.0 while maintaining stability across 0–30 °C and pH 6.6–9.6. Its distinctive halotolerant properties included full activity retention in 0.6 M NaCl and >60% efficiency in salt-free conditions. The enzyme exhibits tolerance to K+, Ca2+, and Fe³+ while demonstrating specific inhibition by Cu2+/Zn2+. With its heterologously validated functional properties, Alphaz emerges as a programmable enzymatic tool offering advantages in sustained-release formulation quality control, targeted prodrug modification, and precision medicine applications, thereby enabling sustainable biomanufacturing solutions that harmonize process reliability with environmental compatibility. Full article
(This article belongs to the Special Issue Advances of Marine-Derived Enzymes)
►▼ Show Figures

Figure 1

15 pages, 4338 KiB  
Article
Multi-Functional Alginate Lyase AlgVR7 from Vibrio rumoiensis: Structural Insights and Catalytic Mechanisms
by Zhe Huang, Shuai Liang, Wulong Jiang, Li Wang, Yuan Wang, Hua Wang, Lianshun Wang, Yuting Cong, Yanan Lu and Guojun Yang
Mar. Drugs 2025, 23(3), 124; https://doi.org/10.3390/md23030124 - 13 Mar 2025
Viewed by 708
Abstract
In this study, we identified AlgVR7, a novel bifunctional alginate lyase from Vibrio rumoiensis and characterized its biochemical properties and substrate specificity. Sequence alignment analysis inferred the key residues K267, H162, N86, E189, and T244 for AlgVR7 catalysis, and it is derived [...] Read more.
In this study, we identified AlgVR7, a novel bifunctional alginate lyase from Vibrio rumoiensis and characterized its biochemical properties and substrate specificity. Sequence alignment analysis inferred the key residues K267, H162, N86, E189, and T244 for AlgVR7 catalysis, and it is derived from the PL7 family; exhibited high activity towards sodium alginate, polyM (PM), and polyG (PG); and can also degrade polygalacturonic acid (PGA) efficiently, with the highest affinity and catalytic efficiency for the MG block of the substrate. The optimal temperature and pH for AlgVR7 were determined to be 40 °C and pH 8, respectively. The enzyme activity of AlgVR7 was maximum at 40 °C, 40% of the enzyme activity was retained after incubation at 60 °C for 60 min, and enzyme activity was still present after 60 min incubation. AlgVR7 activity was stimulated by 100 Mm NaCl, indicating a halophilic nature and suitability for marine environments. Degradation products analyzed using ESI-MS revealed that the enzyme primarily produced trisaccharides and tetrasaccharides. At 40 °C and pH 8.0, its Km values for sodium alginate, PM, and PG were 16.67 μmol, 13.12 μmol, and 22.86 μmol, respectively. Structural analysis and molecular docking studies unveiled the key catalytic residues involved in substrate recognition and interaction. Glu167 was identified as a critical residue for the PL7_5 subfamily, uniquely playing an essential role in alginate decomposition. Overall, AlgVR7 exhibits great potential as a powerful bifunctional enzyme for the efficient preparation of alginate oligosaccharides, with promising applications in biotechnology and industrial fields. Full article
(This article belongs to the Special Issue Advances of Marine-Derived Enzymes)
►▼ Show Figures

Figure 1

28 pages, 6511 KiB  
Article
Identification and Characterization of Two Aryl Sulfotransferases from Deep-Sea Marine Fungi and Their Implications in the Sulfation of Secondary Metabolites
by Nicolas Graziano, Beatriz Arce-López, Tristan Barbeyron, Ludovic Delage, Elise Gerometta, Catherine Roullier, Gaëtan Burgaud, Elisabeth Poirier, Laure Martinelli, Jean-Luc Jany, Nolwenn Hymery and Laurence Meslet-Cladiere
Mar. Drugs 2024, 22(12), 572; https://doi.org/10.3390/md22120572 - 20 Dec 2024
Viewed by 1401
Abstract
Sulfation plays a critical role in the biosynthesis of small molecules, regulatory mechanisms such as hormone signaling, and detoxification processes (phase II enzymes). The sulfation reaction is catalyzed by a broad family of enzymes known as sulfotransferases (SULTs), which have been extensively studied [...] Read more.
Sulfation plays a critical role in the biosynthesis of small molecules, regulatory mechanisms such as hormone signaling, and detoxification processes (phase II enzymes). The sulfation reaction is catalyzed by a broad family of enzymes known as sulfotransferases (SULTs), which have been extensively studied in animals due to their medical importance, but also in plant key processes. Despite the identification of some sulfated metabolites in fungi, the mechanisms underlying fungal sulfation remain largely unknown. To address this knowledge gap, we conducted a comprehensive search of available genomes, resulting in the identification of 174 putative SULT genes in the Ascomycota phylum. Phylogenetic analysis and structural modeling revealed that these SULTs belong to the aryl sulfotransferase family, and they are divided into two potential distinct clusters of PAPS-dependent SULTs within the fungal kingdom. SULT genes from two marine fungi isolated from deep-sea hydrothermal vents, Hortaea werneckii UBOCC-A-208029 (HwSULT) and Aspergillus sydowii UBOCC-A-108050 SULT (AsSULT), were selected as representatives of each cluster. Recombinant proteins were expressed in Escherichia coli and biochemically characterized. HwSULT demonstrated high and versatile activity, while AsSULT appeared more substrate-specific. Here, HwSULT was used to sulfate the mycotoxin zearalenone, enhancing its cytotoxicity toward healthy feline intestinal cells. Full article
(This article belongs to the Special Issue Advances of Marine-Derived Enzymes)
►▼ Show Figures

Figure 1

11 pages, 2492 KiB  
Article
Lichenase and Cellobiohydrolase Activities of a Novel Bi-Functional β-Glucanase from the Marine Bacterium Streptomyces sp. J103
by Youngdeuk Lee, Eunyoung Jo, Yeon-Ju Lee, Min Jin Kim, Navindu Dinara Gajanayaka, Mahanama De Zoysa, Gun-Hoo Park and Chulhong Oh
Mar. Drugs 2024, 22(12), 558; https://doi.org/10.3390/md22120558 - 13 Dec 2024
Viewed by 1223
Abstract
In this study, we report the molecular and enzymatic characterisation of Spg103, a novel bifunctional β-glucanase from the marine bacterium Streptomyces sp. J103. Recombinant Spg103 (rSpg103) functioned optimally at 60 °C and pH 6. Notably, Spg103 exhibited distinct stability properties, with increased activity [...] Read more.
In this study, we report the molecular and enzymatic characterisation of Spg103, a novel bifunctional β-glucanase from the marine bacterium Streptomyces sp. J103. Recombinant Spg103 (rSpg103) functioned optimally at 60 °C and pH 6. Notably, Spg103 exhibited distinct stability properties, with increased activity in the presence of Na+ and EDTA. Spg103 displays both lichenase and cellobiohydrolase activity. Despite possessing a GH5 cellulase domain, FN3 and CBM3 domains characteristic of cellulases and CBHs, biochemical assays showed that rSpg103 exhibited higher activity towards mixed β-1,3-1,4-glucan such as barley β-glucan and lichenan than towards beta-1,4-linkages. The endolytic activity of the enzyme was confirmed by TLC and UPLC-MS analyses, which identified cellotriose as the main hydrolysis product. In addition, Spg103 exhibited an exo-type activity, selectively releasing cellobiose units from cellooligosaccharides, which is characteristic of cellobiohydrolases. These results demonstrate the potential of Spg103 for a variety of biotechnological applications, particularly those requiring tailor-made enzymatic degradation of mixed-linked β-glucans. This study provides a basis for further structural and functional investigations of the bifunctional enzyme and highlights Spg103 as a promising candidate for industrial applications. Full article
(This article belongs to the Special Issue Advances of Marine-Derived Enzymes)
►▼ Show Figures

Graphical abstract

13 pages, 4082 KiB  
Article
Odd-Numbered Agaro-Oligosaccharides Produced by α-Neoagaro-Oligosaccharide Hydrolase Exert Antioxidant Activity in Human Dermal Fibroblasts
by Eunyoung Jo, Navindu Dinara Gajanayaka, Minthari Sakethanika Bandara, Svini Dileepa Marasinghe, Gun-Hoo Park, Su-Jin Lee, Chulhong Oh and Youngdeuk Lee
Mar. Drugs 2024, 22(11), 495; https://doi.org/10.3390/md22110495 - 3 Nov 2024
Viewed by 1638
Abstract
Agarases produce agar oligosaccharides with various structures exhibiting diverse physiological activities. α-Neoagaro-oligosaccharide hydrolase (α-NAOSH) specifically cleaves even-numbered neoagaro-oligosaccharides, producing 3,6-anhydro-l-galactose (l-AHG) and odd-numbered agaro-oligosaccharides (OAOSs). In this study, α-NAOSH from the agar-degrading marine bacterium Gilvimarinus agarilyticus JEA5 (Gaa117) was [...] Read more.
Agarases produce agar oligosaccharides with various structures exhibiting diverse physiological activities. α-Neoagaro-oligosaccharide hydrolase (α-NAOSH) specifically cleaves even-numbered neoagaro-oligosaccharides, producing 3,6-anhydro-l-galactose (l-AHG) and odd-numbered agaro-oligosaccharides (OAOSs). In this study, α-NAOSH from the agar-degrading marine bacterium Gilvimarinus agarilyticus JEA5 (Gaa117) was purified and characterized using an E. coli expression system to produce OAOSs and determine their bioactivity. Recombinant Gaa117 (rGaa117) showed maximum activity at pH 6.0 and 35 °C. rGaa117 retained >80% of its initial activity after 120 min at 30 °C. The activity was enhanced in the presence of Mn2+. Km, Vmax, and Kcat/Km values of the enzyme were 22.64 mM, 246.3 U/mg, and 15 s−1/mM, respectively. rGaa117 hydrolyzed neoagarobiose, neoagarotetraose, and neoagarohexaose, producing OAOSs that commonly contained l-AHG. Neoagarobiose and neoagarotetraose mixtures, designated NAO24, and mixtures of l-AHG and agarotriose, designated AO13, were obtained using recombinant rGaa16B (β-agarase) and rGaa117, respectively, and their antioxidant activities were compared. AO13 showed higher hydrogen peroxide-scavenging activity than NAO24 in human dermal fibroblasts in vitro because of structural differences: AOSs have d-galactose at the non-reducing end, whereas NAOSs have l-AHG. In conclusion, OAOSs exhibited high ROS-scavenging activity in H2O2-induced human dermal fibroblasts. They may be applicable in cosmetics and pharmaceuticals for prevention of skin aging. Full article
(This article belongs to the Special Issue Advances of Marine-Derived Enzymes)
►▼ Show Figures

Figure 1

14 pages, 5606 KiB  
Article
Enantioselectivity in Vanadium-Dependent Haloperoxidases of Different Marine Sources for Sulfide Oxidation to Sulfoxides
by Yun-Han Zhang, Ya-Ting Zou, Yong-Yi Zeng, Lan Liu and Bi-Shuang Chen
Mar. Drugs 2024, 22(9), 419; https://doi.org/10.3390/md22090419 - 14 Sep 2024
Viewed by 1274
Abstract
This study explores the reasons behind the variations in the enantioselectivity of the sulfoxidation of methyl phenyl sulfide by marine-derived vanadium-dependent haloperoxidases (VHPOs). Twelve new VHPOs of marine organisms were overexpressed, purified, and tested for their ability to oxidize sulfide. Most of these [...] Read more.
This study explores the reasons behind the variations in the enantioselectivity of the sulfoxidation of methyl phenyl sulfide by marine-derived vanadium-dependent haloperoxidases (VHPOs). Twelve new VHPOs of marine organisms were overexpressed, purified, and tested for their ability to oxidize sulfide. Most of these marine enzymes exhibited nonenantioselective behavior, underscoring the uniqueness of AnVBPO from the brown seaweed Ascophyllum nodosum and CpVBPO from the red seaweed Corallina pilulifera, which produce (R)- and (S)-sulfoxides, respectively. The enantioselective sulfoxidation pathway is likely due to direct oxygen transfer within the VHPO active site. This was demonstrated through molecular docking and molecular dynamics simulations, which revealed differences in the positioning of sulfide within AnVBPO and CpVBPO, thus explaining their distinct enantioselectivities. Nonenantioselective VHPOs probably follow a different oxidation pathway, initiating with sulfide oxidation to form a positively charged radical. Further insights were gained from studying the catalytic effect of VO43− on H2O2-driven sulfoxidation. This research improves the understanding of VHPO-mediated sulfoxidation and aids in developing biocatalysts for sulfoxide synthesis. Full article
(This article belongs to the Special Issue Advances of Marine-Derived Enzymes)
►▼ Show Figures

Figure 1

13 pages, 2442 KiB  
Article
Purification and Characterization of a Novel Fibrinolytic Enzyme from Marine Bacterium Bacillus sp. S-3685 Isolated from the South China Sea
by Zibin Ma, Jeevithan Elango, Jianhua Hao and Wenhui Wu
Mar. Drugs 2024, 22(6), 267; https://doi.org/10.3390/md22060267 - 10 Jun 2024
Viewed by 1765
Abstract
A novel fibrinolytic enzyme, BSFE1, was isolated from the marine bacterium Bacillus sp. S-3685 (GenBank No.: KJ023685) found in the South China Sea. This enzyme, with a molecular weight of approximately 42 kDa and a specific activity of 736.4 U/mg, exhibited its highest [...] Read more.
A novel fibrinolytic enzyme, BSFE1, was isolated from the marine bacterium Bacillus sp. S-3685 (GenBank No.: KJ023685) found in the South China Sea. This enzyme, with a molecular weight of approximately 42 kDa and a specific activity of 736.4 U/mg, exhibited its highest activity at 37 °C in a phosphate buffer at pH 8.0. The fibrinolytic enzyme remained stable over a pH range of 7.5 to 10.0 and retained about 76% of its activity after being incubated at 37 °C for 2 h. The Km and Vmax values of the enzyme at 37 °C were determined to be 2.1 μM and 49.0 μmol min−1 mg−1, respectively. The fibrinolytic activity of BSFE1 was enhanced by Na+, Ba2+, K+, Co2+, Mn2+, Al3+, and Cu2+, while it was inhibited by Fe3+, Ca2+, Mg2+, Zn2+, and Fe2+. These findings indicate that the fibrinolytic enzyme isolated in this study exhibits a strong affinity for fibrin. Moreover, the enzyme we have purified demonstrates thrombolytic enzymatic activity. These characteristics make BSFE1 a promising candidate for thrombolytic therapy. In conclusion, the results obtained from this study suggest that our work holds potential in the development of agents for thrombolytic treatment. Full article
(This article belongs to the Special Issue Advances of Marine-Derived Enzymes)
►▼ Show Figures

Figure 1

Review

Jump to: Research

23 pages, 2756 KiB  
Review
The Origin, Properties, Structure, Catalytic Mechanism, and Applications of Fucoidan-Degrading Enzymes
by Yi Zhao, Limin Ning, Penghui Zhu, Jinju Jiang, Zhong Yao and Benwei Zhu
Mar. Drugs 2025, 23(3), 97; https://doi.org/10.3390/md23030097 - 23 Feb 2025
Viewed by 871
Abstract
Fucoidanase is a class of enzymes capable of hydrolyzing fucoidan, a complex sulfated polysaccharide found mainly in marine brown algae and some marine invertebrates. Fucoidan (FUC) has a wide range of potential health benefits and therapeutic effects, including antitumor, immunomodulatory, antiviral, and hypoglycemic [...] Read more.
Fucoidanase is a class of enzymes capable of hydrolyzing fucoidan, a complex sulfated polysaccharide found mainly in marine brown algae and some marine invertebrates. Fucoidan (FUC) has a wide range of potential health benefits and therapeutic effects, including antitumor, immunomodulatory, antiviral, and hypoglycemic activities. Fucoidanase can hydrolyze high-molecular-weight fucoidan into medium- and low-molecular-weight fucoidan. The low-molecular-weight fucoidan not only has good solubility, low viscosity, and high absorption rate but also retains the original biological activities of fucoidan. Fucoidanase has received much attention in recent years. This paper reviews the taxonomic origin, structure, enzymatic properties, and applications of fucoidanase to provide a reference for the study of fucoidanase. Full article
(This article belongs to the Special Issue Advances of Marine-Derived Enzymes)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-8
Back to TopTop