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Marine Drugs
Special Issues
Marine Functional Carbohydrates: Enzymatic Manufacturing and Activity Evaluation
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Marine Functional Carbohydrates: Enzymatic Manufacturing and Activity Evaluation

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 December 2024 | Viewed by 4317

Special Issue Editor

Dr. Heng Li

E-Mail Website
Guest Editor
Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, China
Interests: enzymes in glycan modification; functional glycan biosynthesis; bioactivity evaluation; probiotics excavation and engineering

Special Issue Information

Dear Colleagues,

Marine functional carbohydrates present vast opportunities for nutraceutical, medicine, and food discovery. In order to fully utilize and exploit these resources, biological tools including enzymes and microorganisms can be employed to exert effective and efficient impacts on carbohydrate acquisition and glycan processing. Recent advances in DNA sequencing and high-thoughput screening have led to significant developments in the exploration of novel efficient biocatalysts. In addition, omics research such as genomics and metabolomics also promote activity evaluation studies at a deeper level using cell and animal models.

For this Special Issue, we invite original research articles and reviews that highlight both the biocatalysts used for the manufacturing of marine functional carbohydrates and the biological activity assessment of known or novel marine carbohydrates.

Dr. Heng Li
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

  • enzyme characterization
  • enzyme expression and modification
  • microorganism isolation and optimization
  • carbohydrate manufacturing with enzyme/microorganisms
  • marine polysaccharides and oligosaccharides
  • activity evaluation
  • cell and animal model
  • impact on microflora or specific microorganisms
  • omics research
  • mechanism analysis

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

Published Papers (3 papers)

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Research

16 pages, 3244 KiB  
Article
Genome Analysis of a Potential Novel Vibrio Species Secreting pH- and Thermo-Stable Alginate Lyase and Its Application in Producing Alginate Oligosaccharides
by Ke Bao, Miao Yang, Qianhuan Sun, Kaishan Zhang and Huiqin Huang
Mar. Drugs 2024, 22(9), 414; https://doi.org/10.3390/md22090414 - 10 Sep 2024
Viewed by 1159
Abstract
Alginate lyase is an attractive biocatalyst that can specifically degrade alginate to produce oligosaccharides, showing great potential for industrial and medicinal applications. Herein, an alginate-degrading strain HB236076 was isolated from Sargassum sp. in Qionghai, Hainan, China. The low 16S rRNA gene sequence identity [...] Read more.
Alginate lyase is an attractive biocatalyst that can specifically degrade alginate to produce oligosaccharides, showing great potential for industrial and medicinal applications. Herein, an alginate-degrading strain HB236076 was isolated from Sargassum sp. in Qionghai, Hainan, China. The low 16S rRNA gene sequence identity (<98.4%), ANI value (<71.9%), and dDDH value (<23.9%) clearly indicated that the isolate represented a potential novel species of the genus Vibrio. The genome contained two chromosomes with lengths of 3,007,948 bp and 874,895 bp, respectively, totaling 3,882,843 bp with a G+C content of 46.5%. Among 3482 genes, 3332 protein-coding genes, 116 tRNA, and 34 rRNA sequences were predicted. Analysis of the amino acid sequences showed that the strain encoded 73 carbohydrate-active enzymes (CAZymes), predicting seven PL7 (Alg1–7) and two PL17 family (Alg8, 9) alginate lyases. The extracellular alginate lyase from strain HB236076 showed the maximum activity at 50 °C and pH 7.0, with over 90% activity measured in the range of 30–60 °C and pH 6.0–10.0, exhibiting a wide range of temperature and pH activities. The enzyme also remained at more than 90% of the original activity at a wide pH range (3.0–9.0) and temperature below 50 °C for more than 2 h, demonstrating significant thermal and pH stabilities. Fe2+ had a good promoting effect on the alginate lyase activity at 10 mM, increasing by 3.5 times. Thin layer chromatography (TLC) and electrospray ionization mass spectrometry (ESI-MS) analyses suggested that alginate lyase in fermentation broth could catalyze sodium alginate to produce disaccharides and trisaccharides, which showed antimicrobial activity against Shigella dysenteriae, Aeromonas hydrophila, Staphylococcus aureus, Streptococcus agalactiae, and Escherichia coli. This research provided extended insights into the production mechanism of alginate lyase from Vibrio sp. HB236076, which was beneficial for further application in the preparation of pH-stable and thermo-stable alginate lyase and alginate oligosaccharides. Full article
(This article belongs to the Special Issue Marine Functional Carbohydrates: Enzymatic Manufacturing and Activity Evaluation)
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17 pages, 6491 KiB  
Article
Identification and Characterization of a Highly Active Hyaluronan Lyase from Enterobacter asburiae
by Linjing Zhang, Jiayu Jiang, Wei Liu, Lianlong Wang, Zhiyuan Yao, Heng Li, Jinsong Gong, Chuanli Kang, Lei Liu, Zhenghong Xu and Jinsong Shi
Mar. Drugs 2024, 22(9), 399; https://doi.org/10.3390/md22090399 - 31 Aug 2024
Viewed by 1152
Abstract
Hyaluronic acid (HA) is a well-known functional marine polysaccharide. The utilization and derivative development of HA are of great interest. Hyaluronan lyase has wide application prospects in the production of HA oligosaccharides and lower molecular weight HA. In this study, a strain of [...] Read more.
Hyaluronic acid (HA) is a well-known functional marine polysaccharide. The utilization and derivative development of HA are of great interest. Hyaluronan lyase has wide application prospects in the production of HA oligosaccharides and lower molecular weight HA. In this study, a strain of Enterobacter asburiae CGJ001 with high hyaluronan lyase activity was screened from industrial wastewater. This strain exhibited an impressive enzyme activity of 40,576 U/mL after being incubated for 14 h. Whole genome sequencing analysis revealed that E. asburiae CGJ001 contained a cluster of genes involved in HA degradation, transport, and metabolism. A newly identified enzyme responsible for glycosaminoglycan degradation was designated as HylEP0006. A strain of E. coli BL21(DE3)/pET-22b(+)-hylEP0006 was successfully constructed. HylEP0006 exhibited optimal degradation at 40 °C and pH 7.0, showing a high activity of 950,168.3 U/mg. HylEP0006 showed specific activity against HA. The minimum degradation fragment of HylEP0006 was hyaluronan tetrasaccharides, and HylEP0006 could efficiently degrade HA into unsaturated disaccharides (HA2), with HA2 as the final product. These characteristics indicate that HylEP0006 has a potential application prospect for the extraction and utilization of hyaluronic acid. Full article
(This article belongs to the Special Issue Marine Functional Carbohydrates: Enzymatic Manufacturing and Activity Evaluation)
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16 pages, 5380 KiB  
Article
High-Level Extracellular Production of a Trisaccharide-Producing Alginate Lyase AlyC7 in Escherichia coli and Its Agricultural Application
by Xiao-Han Wang, Yu-Qiang Zhang, Xin-Ru Zhang, Xiao-Dong Zhang, Xiao-Meng Sun, Xiao-Fei Wang, Xiao-Hui Sun, Xiao-Yan Song, Yu-Zhong Zhang, Ning Wang, Xiu-Lan Chen and Fei Xu
Mar. Drugs 2024, 22(5), 230; https://doi.org/10.3390/md22050230 - 18 May 2024
Viewed by 1618
Abstract
Alginate oligosaccharides (AOS), products of alginate degradation by endotype alginate lyases, possess favorable biological activities and have broad applications. Although many have been reported, alginate lyases with homogeneous AOS products and secretory production by an engineered host are scarce. Herein, the alginate lyase [...] Read more.
Alginate oligosaccharides (AOS), products of alginate degradation by endotype alginate lyases, possess favorable biological activities and have broad applications. Although many have been reported, alginate lyases with homogeneous AOS products and secretory production by an engineered host are scarce. Herein, the alginate lyase AlyC7 from Vibrio sp. C42 was characterized as a trisaccharide-producing lyase exhibiting high activity and broad substrate specificity. With PelB as the signal peptide and 500 mM glycine as the additive, the extracellular production of AlyC7 in Escherichia coli reached 1122.8 U/mL after 27 h cultivation in Luria-Bertani medium. The yield of trisaccharides from sodium alginate degradation by the produced AlyC7 reached 758.6 mg/g, with a purity of 85.1%. The prepared AOS at 20 μg/mL increased the root length of lettuce, tomato, wheat, and maize by 27.5%, 25.7%, 9.7%, and 11.1%, respectively. This study establishes a robust foundation for the industrial and agricultural applications of AlyC7. Full article
(This article belongs to the Special Issue Marine Functional Carbohydrates: Enzymatic Manufacturing and Activity Evaluation)
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