Advances in Marine Polysaccharide Modifying Enzymes: Discovery, Characterization, Structure, Modification and Applications

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: closed (29 February 2024) | Viewed by 6762

Special Issue Editors


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Guest Editor
Faculty of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611, Japan
Interests: enzymatic character of marine organisms and microorganisms; exploitation of utilization of marine algae; development of genome editing method for marine algae
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Guest Editor
Faculty of Fisheries Sciences, Hokkaido University Hakodate, Hokkaido, Japan
Interests: red algae; marine invertebrates; phycoerythrin; xyloorigosaccharide; marine enzymes; marine collagen; chloroplast DNA; antihypertension; prebiotics; antioxidation; antidiabetes
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Guest Editor
College of Food Science and light Industry, Nanjing Tech University, Nanjing, China
Interests: discovering, enzymatic and structural characterization; novel marine polysaccharide-degrading enzymes
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Special Issue Information

Dear Colleagues,

Due to global climate change, environmental issues have become more conscious. Seaweed plays a major role in blue carbon, which fixes carbon to the ocean by taking in carbon dioxide through photosynthesis and producing polysaccharides. In addition to environmental problems, marine polysaccharides have various modifying groups and have been found to have different functionality from land plants. Marine polysaccharides have been used in foods and medicines. Recently, novel biocatalysis of polysaccharide-relating enzymes has been discovered. As a result, the functionality of oligosaccharides from marine polysaccharides has been clarified, e.g., health functionality such as anticancer, anti-inflammatory effect, intestinal regulation and antioxidant activity. This Special Issue aims to accumulate the knowledge of discovery, preparation, function, structure, modification and application of bioactive oligosaccharides- and polysaccharides-modifying enzymes from marine organisms. This Special Issue aims to contribute to the achievement of multiple goals of Sustainable Development Goals (SDGs) (No. 2, 3, 12, 14), and we would like to invite scientists to submit their latest research findings in this field. Comprehensive review papers are also welcome.

Dr. Yuya Kumagai
Prof. Dr. Hideki Kishimura
Prof. Dr. Benwei Zhu
Guest Editors

Manuscript Submission Information

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Keywords

  • marine biotechnology
  • marine organism
  • enzyme kinetics
  • crystal structure
  • structure modification
  • directed evolution
  • rational design
  • biocatalysis
  • polysaccharide
  • carbohydrate recognition.

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Published Papers (4 papers)

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Research

14 pages, 2502 KiB  
Article
Production of Alginate Oligosaccharides (AOSs) Using Enhanced Physicochemical Properties of Immobilized Alginate Lyase for Industrial Application
by Simranjeet Kaur, Reinu E. Abraham, Christopher M. M. Franco and Munish Puri
Mar. Drugs 2024, 22(3), 120; https://doi.org/10.3390/md22030120 - 04 Mar 2024
Viewed by 1279
Abstract
Alginate lyase (AL) is a polysaccharide-degrading enzyme that can degrade alginate by hydrolyzing glycosidic bonds and produces unsaturated alginate oligosaccharides (AOSs). These AOSs have wide therapeutic and nutraceutical applications. However, to produce alginate oligosaccharides in a cost-effective manner is challenging due to the [...] Read more.
Alginate lyase (AL) is a polysaccharide-degrading enzyme that can degrade alginate by hydrolyzing glycosidic bonds and produces unsaturated alginate oligosaccharides (AOSs). These AOSs have wide therapeutic and nutraceutical applications. However, to produce alginate oligosaccharides in a cost-effective manner is challenging due to the low availability and high cost of this degrading enzyme. Immobilization of the enzyme facilitates industrial applications owing to its stability, reusability, and cost-effectiveness. This study was focused on the enhancement of the properties of alginate lyase and improvement of the production of AOS. Alginate lyase was immobilized on magnetic nanoparticles (NPs) using glutaraldehyde as the crosslinker. The study showed that the maximum binding achieved between NPs and protein in the enzyme was 71% at a ratio of 1:150 NP:protein. As a result of immobilization, the optimum activity of free enzyme which was obtained at 37 °C and pH 7.4 changed to 45 °C and pH 9. Furthermore, the enzyme was thermostable at 45 °C for 3 h with up to 50% reusability for six consecutive cycles. Storage stability after 15 days showed ~67% relative hydrolysis of alginate. The free alginate lyase (25 IU) showed 76% raw biomass (seaweed) hydrolysis which is higher compared to 63% provided by the immobilized enzyme. As a result of efficient hydrolysis, AOSs with molecular weight profile of 370–1040 kDa were produced and detected using HPLC. Full article
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22 pages, 11541 KiB  
Article
Cloning and Characterization of a Novel N-Acetyl-D-galactosamine-4-O-sulfate Sulfatase, SulA1, from a Marine Arthrobacter Strain
by Monica Daugbjerg Christensen, Leila Allahgholi, Javier A. Linares-Pastén, Ólafur Friðjónsson, Hörður Guðmundsson, Varsha Kale, Roya R. R. Sardari, Guðmundur Ó. Hreggviðsson and Eva Nordberg Karlsson
Mar. Drugs 2024, 22(3), 104; https://doi.org/10.3390/md22030104 - 23 Feb 2024
Viewed by 2556
Abstract
Sulfation is gaining increased interest due to the role of sulfate in the bioactivity of many polysaccharides of marine origin. Hence, sulfatases, enzymes that control the degree of sulfation, are being more extensively researched. In this work, a novel sulfatase (SulA1) encoded by [...] Read more.
Sulfation is gaining increased interest due to the role of sulfate in the bioactivity of many polysaccharides of marine origin. Hence, sulfatases, enzymes that control the degree of sulfation, are being more extensively researched. In this work, a novel sulfatase (SulA1) encoded by the gene sulA1 was characterized. The sulA1-gene is located upstream of a chondroitin lyase encoding gene in the genome of the marine Arthrobacter strain (MAT3885). The sulfatase was produced in Escherichia coli. Based on the primary sequence, the enzyme is classified under sulfatase family 1 and the two catalytic residues typical of the sulfatase 1 family—Cys57 (post-translationally modified to formyl glycine for function) and His190—were conserved. The enzyme showed increased activity, but not improved stability, in the presence of Ca2+, and conserved residues for Ca2+ binding were identified (Asp17, Asp18, Asp277, and Asn278) in a structural model of the enzyme. The temperature and pH activity profiles (screened using p-nitrocatechol sulfate) were narrow, with an activity optimum at 40–50 °C and a pH optimum at pH 5.5. The Tm was significantly higher (67 °C) than the activity optimum. Desulfation activity was not detected on polymeric substrates, but was found on GalNAc4S, which is a sulfated monomer in the repeated disaccharide unit (GlcA–GalNAc4S) of, e.g., chondroitin sulfate A. The position of the sulA1 gene upstream of a chondroitin lyase gene and combined with the activity on GalNAc4S suggests that there is an involvement of the enzyme in the chondroitin-degrading cascade reaction, which specifically removes sulfate from monomeric GalNAc4S from chondroitin sulfate degradation products. Full article
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17 pages, 9412 KiB  
Article
Genome Sequencing-Based Mining and Characterization of a Novel Alginate Lyase from Vibrio alginolyticus S10 for Specific Production of Disaccharides
by Zhiqiang Shu, Gongming Wang, Fang Liu, Yingjiang Xu, Jianan Sun, Yang Hu, Hao Dong and Jian Zhang
Mar. Drugs 2023, 21(11), 564; https://doi.org/10.3390/md21110564 - 27 Oct 2023
Viewed by 1167
Abstract
Alginate oligosaccharides prepared by alginate lyases attracted great attention because of their desirable biological activities. However, the hydrolysis products are always a mixture of oligosaccharides with different degrees of polymerization, which increases the production cost because of the following purification procedures. In this [...] Read more.
Alginate oligosaccharides prepared by alginate lyases attracted great attention because of their desirable biological activities. However, the hydrolysis products are always a mixture of oligosaccharides with different degrees of polymerization, which increases the production cost because of the following purification procedures. In this study, an alginate lyase, Alg4755, with high product specificity was identified, heterologously expressed, and characterized from Vibrio alginolyticus S10, which was isolated from the intestine of sea cucumber. Alg4755 belonged to the PL7 family with two catalytic domains, which was composed of 583 amino acids. Enzymatic characterization results show that the optimal reaction temperature and pH of Alg4755 were 35 °C and 8.0, respectively. Furthermore, Alg4755 was identified to have high thermal and pH stability. Moreover, the final hydrolysis products of sodium alginate catalyzed by Alg4755 were mainly alginate disaccharides with a small amount of alginate trisaccharides. The results demonstrate that alginate lyase Alg4755 could have a broad application prospect because of its high product specificity and desirable catalytic properties. Full article
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16 pages, 4713 KiB  
Article
Biochemical Properties of a Cold-Active Chitinase from Marine Trichoderma gamsii R1 and Its Application to Preparation of Chitin Oligosaccharides
by Jianrong Wang, Mujin Zhu, Ping Wang and Wei Chen
Mar. Drugs 2023, 21(6), 332; https://doi.org/10.3390/md21060332 - 29 May 2023
Cited by 2 | Viewed by 1166
Abstract
The enzymatic degradation of different chitin polymers into chitin oligosaccharides (COSs) is of great significance given their better solubility and various biological applications. Chitinase plays a pivotal role in the enzymatic preparation of COSs. Herein, a cold-adapted and efficient chitinase (ChiTg) from the [...] Read more.
The enzymatic degradation of different chitin polymers into chitin oligosaccharides (COSs) is of great significance given their better solubility and various biological applications. Chitinase plays a pivotal role in the enzymatic preparation of COSs. Herein, a cold-adapted and efficient chitinase (ChiTg) from the marine Trichoderma gamsii R1 was purified and characterized. The optimal temperature of ChiTg was 40 °C, and the relative activity at 5 °C was above 40.1%. Meanwhile, ChiTg was active and stable from pH 4.0 to 7.0. As an endo-type chitinase, ChiTg exhibited the highest activity with colloidal chitin, then with ball-milled and powdery chitin. In addition, ChiTg showed high efficiency when hydrolyzing colloidal chitin at different temperatures, and the end products were mainly composed of COSs with one to three degrees of polymerization. Furthermore, the results of bioinformatics analysis revealed that ChiTg belongs to the GH18 family, and its acidic surface and the flexible structure of its catalytic site may contribute to its high activity in cold conditions. The results of this study provide a cold-active and efficient chitinase and ideas for its application regarding the preparation of COSs from colloidal chitin. Full article
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