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Marine-Derived Polysaccharide-Degrading Enzyme

A special issue of Marine Drugs (ISSN 1660-3397). This special issue belongs to the section "Marine-Derived Ingredients for Drugs, Cosmeceuticals and Nutraceuticals".

Deadline for manuscript submissions: 15 November 2026 | Viewed by 961

Special Issue Editor

School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
Interests: biocatalysis; structure-function relationship of enzyme; biofilm; synthetic biology

Special Issue Information

Dear Colleagues,

Marine ecosystems are abundant with with high-value polysaccharides, such as alginate (from brown algae), agar/agarose and carrageenan (from red algae), ulvan (from green algae), and hyaluromic acid and chondroitin sulfate (from animals), which serve as critical resources for food, pharmaceuticals, and biorefineries. Marine-derived polysaccharide-degrading enzymes, involved in the flux of matter and energy in the global oceans, are major drivers of global biogeochemical cycling. They also have been applied in the production of pharmaceuticals, health supplements and foods through catalyzing polysaccharide degradation into bioactive oligosaccharides.

This Special Issue invites original research and reviews on the isolation, genomic/metabolomic analysis of the producers, characterization, catalytic mechanisms, fermentation and industrial applications of marine-derived polysaccharide-degrading enzymes.

Dr. Feng Han
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 250 words) can be sent to the Editorial Office for assessment.

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-derived polysaccharide-degrading enzyme
  • marine polysaccharide
  • marine oligosaccharide
  • marine microorganism
  • genome mining
  • structure–function relationship
  • industrial application

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Published Papers (1 paper)

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Research

19 pages, 4509 KB  
Article
Molecular Characterization and Mechanistic Insights of a Thermostable Neoagarobiose Hydrolase Aga2457 from Alteromonas sp.
by Jiang Li, Xinning Pan, Long Chen, Qian Zhang, Zhiyan Wang, Dewi Seswita Zilda and Zhou Zheng
Mar. Drugs 2026, 24(4), 123; https://doi.org/10.3390/md24040123 - 25 Mar 2026
Viewed by 639
Abstract
The enzymatic valorization of agarose, a major polysaccharide in red algae, is critical for its application in the food, pharmaceutical, and biotechnology industries. In this study, a gene encoding a thermostable α-neoagarobiose hydrolase, aga2457, was cloned from an epiphytic bacterium associated with [...] Read more.
The enzymatic valorization of agarose, a major polysaccharide in red algae, is critical for its application in the food, pharmaceutical, and biotechnology industries. In this study, a gene encoding a thermostable α-neoagarobiose hydrolase, aga2457, was cloned from an epiphytic bacterium associated with Indonesian macroalgae. Unlike typical mesophilic GH117 enzymes, recombinant Aga2457 displayed a higher optimal temperature at 50 °C and retained 55% activity after 12 days of incubation at 50 °C. The enzyme specifically hydrolyzes neoagarobiose into D-galactose and 3,6-anhydro-L-galactose, thereby facilitating the complete depolymerization of agarose. Combined molecular dynamics (MD) simulations and site-directed mutagenesis revealed that residues P253, N256, and Q285 are pivotal for substrate recognition and active site stability. These findings highlight Aga2457 as a robust biocatalyst for industrial agar processing and provide structural insights for the rational design of thermostable agarolytic enzymes. Full article
(This article belongs to the Special Issue Marine-Derived Polysaccharide-Degrading Enzyme)
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