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Marine Drugs
Special Issues
Marine Proteins and Enzymes: Bioactivities and Medicinal Applications
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Marine Proteins and Enzymes: Bioactivities and Medicinal Applications

A special issue of Marine Drugs (ISSN 1660-3397). This special issue belongs to the section "Marine Pharmacology".

Deadline for manuscript submissions: 30 November 2024 | Viewed by 5818

Special Issue Editors

Prof. Dr. Min-Jie Cao

E-Mail Website
Guest Editor
College of Ocean Food and Biological Engineering, Jimei University, Xiamen, China
Interests: proteins; proteinases; peptides; marine food processing by-products
Dr. Asami Yoshida

E-Mail Website
Guest Editor
Faculty of Fisheries, Nagasaki University, Nagasaki, Japan
Interests: proteinases; collagen; food processing; molecular chaperones

Special Issue Information

Dear Colleagues,

The ocean provides diverse bioactive compounds such as proteins, peptides, saccharides, and lipids, which are synthesized and processed by enzymes within marine organisms. Marine bioactive compounds have been used to benefit people's lives and health, and in recent years, their applications in functional foods and medicines have attracted much attention.

The Special Issue “Marine Proteins and Enzymes: Bioactivities and Medicinal Applications” focuses on the biosynthesis and bioprocessing of proteins, peptides, oligosaccharides, and lipids from marine organisms to convert them into high-value products using enzymes for applications in functional foods, medicine, and industrial products.

We extend an invitation to you to submit your original research papers and review papers to the Special Issue “Marine Proteins and Enzymes: Bioactivities and Medicinal Applications”. We welcome research on the bioprocessing of marine bioactive compounds from the perspectives of biochemistry, biotechnology, enzymology, and microbiology.

Prof. Dr. Min-Jie Cao
Dr. Asami Yoshida
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

  • proteins
  • proteinases
  • glycolytic enzyme
  • enzymes
  • peptides
  • bioactive compounds
  • bioactivities
  • medicine

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

Published Papers (4 papers)

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Research

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16 pages, 1407 KiB  
Article
The Effects of Agaro-Oligosaccharides Produced by Marine Bacteria (Rheinheimera sp. (HY)) Possessing Agarose-Degrading Enzymes on Myotube Function
by Youshi Huang, Takuya Hirose, Jyh-Ming Tsai and Katsuya Hirasaka
Mar. Drugs 2024, 22(11), 515; https://doi.org/10.3390/md22110515 - 14 Nov 2024
Viewed by 639
Abstract
Agarase and its metabolites are reported to have applications in a variety of fields, but there have been few studies of the effects of agaro-oligosaccharide hydrolysate on muscle function. In this study, we analyzed the functionality of agarase and its metabolites in bacteria [...] Read more.
Agarase and its metabolites are reported to have applications in a variety of fields, but there have been few studies of the effects of agaro-oligosaccharide hydrolysate on muscle function. In this study, we analyzed the functionality of agarase and its metabolites in bacteria isolated from seawater. A bacterium with agar-degrading activity was isolated from Shimabara, Nagasaki, Japan. Through 16S rRNA sequence alignment, it was identified as being closely related to Rheinheimera sp. WMF-1 and was provisionally named Rheinheimera sp. (HY). Crude enzymes derived from this bacterium demonstrated an ability to hydrolyze various polysaccharides, including agar, agarose, and starch, with the highest specificity observed for agarose. The optimum pH and temperature were pH 10 and 50 °C. A glycoside bond specificity analysis of enzymatic activity indicated the cleavage of the α-linkage. Next, we investigated the functional effects of agaro-oligosaccharides on C2C12 myotubes. Treatment with 10–30 kDa oligosaccharides significantly increased the hypertrophy rate, diameter, and expression of myosin heavy-chain genes in C2C12 myotubes. These results indicate that the agaro-oligosaccharides produced by the enzymes identified in this study improve muscle mass, suggesting their potential contribution to muscle function. Full article
(This article belongs to the Special Issue Marine Proteins and Enzymes: Bioactivities and Medicinal Applications)
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14 pages, 2870 KiB  
Article
Direct Preparation of Alginate Oligosaccharides from Brown Algae by an Algae-Decomposing Alginate Lyase AlyP18 from the Marine Bacterium Pseudoalteromonas agarivorans A3
by Xiao-Hui Sun, Xiao-Dong Zhang, Xin-Ru Zhang, Xiao-Fei Wang, Xi-Ying Zhang, Yu-Zhong Zhang, Yu-Qiang Zhang and Fei Xu
Mar. Drugs 2024, 22(11), 483; https://doi.org/10.3390/md22110483 - 26 Oct 2024
Viewed by 708
Abstract
Alginate oligosaccharides (AOs), derived from alginate degradation, exhibit diverse biological activities and hold significant promise in various fields. The enzymatic preparation of AOs relies on alginate lyases, which offers distinct advantages. In contrast to the conventional use of sodium alginate derived from brown [...] Read more.
Alginate oligosaccharides (AOs), derived from alginate degradation, exhibit diverse biological activities and hold significant promise in various fields. The enzymatic preparation of AOs relies on alginate lyases, which offers distinct advantages. In contrast to the conventional use of sodium alginate derived from brown algae as the substrate for the enzymatic preparation of AOs, AO preparation directly from brown algae is more appealing due to its time and energy efficiency. Thus, the identification of potent alginate lyases and cost-effective brown algae substrates is crucial for optimizing AO production. Herein, we identified and characterized an alginate lyase, AlyP18, capable of efficiently decomposing algae, from a marine bacterium Pseudoalteromonas agarivorans A3 based on secretome analysis. AlyP18 is a mesothermal, endo-type and bifunctional alginate lyase with high enzymatic activity. Two brown algae substrates, Laminaria japonica roots and Macrocystis pyrifera, were used for the AO preparation by AlyP18. Upon optimization of AlyP18 hydrolysis parameters, the substrate degradation efficiency and AO production reached 53% and ~32% for L. japonica roots, respectively, and 77% and ~46.5% for M. pyrifera. The generated AOs primarily consisted of dimers to pentamers, with trimers and tetramers being dominant. This study provides an efficient alginate lyase and alternative brown algal feedstock for the bioconversion of high-value AOs from brown algae. Full article
(This article belongs to the Special Issue Marine Proteins and Enzymes: Bioactivities and Medicinal Applications)
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16 pages, 3607 KiB  
Article
Modified Hemocyanins from Rapana thomasiana and Helix aspersa Exhibit Strong Antitumor Activity in the B16F10 Mouse Melanoma Model
by Emiliya Stoyanova, Nikolina Mihaylova, Nikola Ralchev, Silviya Bradyanova, Iliyan Manoylov, Yuliana Raynova, Krassimira Idakieva and Andrey Tchorbanov
Mar. Drugs 2024, 22(10), 462; https://doi.org/10.3390/md22100462 - 7 Oct 2024
Viewed by 1057
Abstract
Melanoma is one of the most common tumors worldwide, and new approaches and antitumor drugs for therapy are being investigated. Among the promising biomolecules of natural origin for antitumor research are gastropodan hemocyanins—highly immunogenic multimeric glycoproteins used as antitumor agents and components of [...] Read more.
Melanoma is one of the most common tumors worldwide, and new approaches and antitumor drugs for therapy are being investigated. Among the promising biomolecules of natural origin for antitumor research are gastropodan hemocyanins—highly immunogenic multimeric glycoproteins used as antitumor agents and components of therapeutic vaccines in human and mouse cancer models. A murine melanoma model established in C57BL/6 mice of the B16F10 cell line was used to study anticancer modified oxidized hemocyanins (Ox-Hcs) that were administered to experimental animals (100 μg/mouse) under different regimens: mild, intensive, and with sensitization. The solid tumor growth, antitumor response, cell infiltration in tumors, and survival were assessed using flow cytometry, ELISA, and cytotoxicity assays. Therapy with Ox-RtH or Ox-HaH resulted in the generation of enhanced specific immune response (increased levels of tumor-infiltrated mature NK cells (CD27+CD11b+) in sensitized groups and of macrophages in the intensively immunized animals) and tumor suppression. Beneficial effects such as delayed tumor incidence and growth as well as prolonged survival of tumor-bearing animals have been observed. High levels of melanoma-specific CTLs that mediate cytotoxic effects on tumor cells; tumor-infiltrating IgM antibodies expected to enhance antibody-dependent cellular cytotoxicity; type M1 macrophages, which stimulate the Th1 response and cytotoxic cells; and proinflammatory cytokines, were also observed after Ox-Hcs administration. The modified Hcs showed strong antitumor properties in different administration regimens in a murine model of melanoma with potential for future application in humans. Full article
(This article belongs to the Special Issue Marine Proteins and Enzymes: Bioactivities and Medicinal Applications)
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Review

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29 pages, 4597 KiB  
Review
From Sea to Lab: Angiotensin I-Converting Enzyme Inhibition by Marine Peptides—Mechanisms and Applications
by Du-Min Jo, Fazlurrahman Khan, Seul-Ki Park, Seok-Chun Ko, Kyung Woo Kim, Dongwoo Yang, Ji-Yul Kim, Gun-Woo Oh, Grace Choi, Dae-Sung Lee and Young-Mog Kim
Mar. Drugs 2024, 22(10), 449; https://doi.org/10.3390/md22100449 - 30 Sep 2024
Viewed by 2997
Abstract
To reveal potent ACE inhibitors, researchers screen various bioactive peptides from several sources, and more attention has been given to aquatic sources. This review summarizes the recent research achievements on marine peptides with ACE-inhibitory action and application. Marine peptides are considered excellent bioactives [...] Read more.
To reveal potent ACE inhibitors, researchers screen various bioactive peptides from several sources, and more attention has been given to aquatic sources. This review summarizes the recent research achievements on marine peptides with ACE-inhibitory action and application. Marine peptides are considered excellent bioactives due to their large structural diversity and unusual bioactivities. The mechanisms by which these marine peptides inhibit ACE include competitive binding to ACEs’ active site, interfering with ACE conformational changes, and avoiding the identification of substrates. The unique 3D attributes of marine peptides confer inhibition advantages toward ACE activity. Because IC50 values of marine peptides’ interaction with ACE are low, structure-based research assumes that the interaction between ACE and peptides increased the therapeutic application. Numerous studies on marine peptides focused on the sustainable extraction of ACE-inhibitory peptides produced from several fish, mollusks, algae, and sponges. Meanwhile, their potential applications and medical benefits are worth investigating and considering. Due to these peptides exhibiting antioxidant, antihypertensive, and even antimicrobial properties simultaneously, their therapeutic potential for cardiovascular disease and other illnesses only increases. In addition, as marine peptides show better pharmacological benefits, they have increased absorption rates and low toxicity and could perhaps be modified for better stability and bioefficacy. Biotechnological advances in peptide synthesis and formulation have greatly facilitated the generation of peptide-based ACE inhibitors from marine sources, which subsequently offer new treatment models. This article gives a complete assessment of the present state of knowledge about marine organism peptides as ACE inhibitors. In addition, it emphasizes the relevance of additional investigation into their mechanisms of action, the optimization of manufacturing processes, and assessment in in vivo, preclinical, and clinical settings, underlining the urgency and value of this study. Using marine peptides for ACE inhibition not only broadens the repertory of bioactive compounds but also shows promise for tackling the global health burden caused by cardiovascular diseases. Full article
(This article belongs to the Special Issue Marine Proteins and Enzymes: Bioactivities and Medicinal Applications)
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