Biochemical characterization of mannuronan C5-epimerase from Saccharina japonica.

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Title: Biochemical characterization of mannuronan C5-epimerase from Saccharina japonica.
Authors: Meng, Xue1,2,3 (AUTHOR), Li, Shuang1,2,3 (AUTHOR), Zhang, Jie1,2 (AUTHOR), Duan, Delin1,2 (AUTHOR) dlduan@qdio.ac.cn
Source: Journal of Oceanology & Limnology. May2026, Vol. 44 Issue 3, p1196-1207. 12p.
Subject Terms: *Epimerization, *Enzymes, *Enzymatic analysis, *Brown algae, *Microbial polysaccharides, *Enzyme specificity, *Saccharina, *Polysaccharides
Abstract: Alginate is a polysaccharide predominantly synthesized by brown algae and bacteria. It is a linear polymer composed of β-D-mannuronic acid (M) and its C5 reverse isomer α-L-guluronic acid (G). Currently, there is a significant demand for high-G-content alginate in the market. Mannuronan C5-epimerase (MC5E) is one important enzyme in the alginate synthesis as it catalyzes epimerization of β-D-mannuronic acid (M) to α-L-guluronic acid (G) at the polyM polymer level. We screened and isolated one high expression MC5E sequence from the Saccharina japonica genome database and demonstrated that SjMC5E1 could epimerize and increase the content of G residues in alginate. Additionally, we detected the mannuronan C5-epimerase activity of SjMC5E1 was optimal at 37 °C in the temperature range of 15–50 °C, the FG was 0.30 and the M/G ratio of alginate was the lowest at 2.32. The biochemical characterization of SjMC5E1 provides valuable insights into its role in alginate biosynthesis, particularly in the conversion of M to G. These findings contribute to a better understanding of the enzymatic mechanisms underlying alginate synthesis and may support future efforts to optimize alginate production. However, further studies are needed to fully explore the potential of SjMC5E1 in tailoring alginates with specific properties for industrial or biomedical applications. [ABSTRACT FROM AUTHOR]
Database: Energy & Power Source
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An: 195072611
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Items – Name: Title
  Label: Title
  Group: Ti
  Data: Biochemical characterization of mannuronan C5-epimerase from Saccharina japonica.
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  Label: Authors
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  Data: <searchLink fieldCode="AR" term="%22Meng%2C+Xue%22">Meng, Xue</searchLink><relatesTo>1,2,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Li%2C+Shuang%22">Li, Shuang</searchLink><relatesTo>1,2,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zhang%2C+Jie%22">Zhang, Jie</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Duan%2C+Delin%22">Duan, Delin</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> dlduan@qdio.ac.cn</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Oceanology+%26+Limnology%22">Journal of Oceanology & Limnology</searchLink>. May2026, Vol. 44 Issue 3, p1196-1207. 12p.
– Name: Subject
  Label: Subject Terms
  Group: Su
  Data: *<searchLink fieldCode="DE" term="%22Epimerization%22">Epimerization</searchLink><br />*<searchLink fieldCode="DE" term="%22Enzymes%22">Enzymes</searchLink><br />*<searchLink fieldCode="DE" term="%22Enzymatic+analysis%22">Enzymatic analysis</searchLink><br />*<searchLink fieldCode="DE" term="%22Brown+algae%22">Brown algae</searchLink><br />*<searchLink fieldCode="DE" term="%22Microbial+polysaccharides%22">Microbial polysaccharides</searchLink><br />*<searchLink fieldCode="DE" term="%22Enzyme+specificity%22">Enzyme specificity</searchLink><br />*<searchLink fieldCode="DE" term="%22Saccharina%22">Saccharina</searchLink><br />*<searchLink fieldCode="DE" term="%22Polysaccharides%22">Polysaccharides</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Alginate is a polysaccharide predominantly synthesized by brown algae and bacteria. It is a linear polymer composed of β-D-mannuronic acid (M) and its C5 reverse isomer α-L-guluronic acid (G). Currently, there is a significant demand for high-G-content alginate in the market. Mannuronan C5-epimerase (MC5E) is one important enzyme in the alginate synthesis as it catalyzes epimerization of β-D-mannuronic acid (M) to α-L-guluronic acid (G) at the polyM polymer level. We screened and isolated one high expression MC5E sequence from the Saccharina japonica genome database and demonstrated that SjMC5E1 could epimerize and increase the content of G residues in alginate. Additionally, we detected the mannuronan C5-epimerase activity of SjMC5E1 was optimal at 37 °C in the temperature range of 15–50 °C, the FG was 0.30 and the M/G ratio of alginate was the lowest at 2.32. The biochemical characterization of SjMC5E1 provides valuable insights into its role in alginate biosynthesis, particularly in the conversion of M to G. These findings contribute to a better understanding of the enzymatic mechanisms underlying alginate synthesis and may support future efforts to optimize alginate production. However, further studies are needed to fully explore the potential of SjMC5E1 in tailoring alginates with specific properties for industrial or biomedical applications. [ABSTRACT FROM AUTHOR]
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RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1007/s00343-025-5173-2
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 12
        StartPage: 1196
    Subjects:
      – SubjectFull: Epimerization
        Type: general
      – SubjectFull: Enzymes
        Type: general
      – SubjectFull: Enzymatic analysis
        Type: general
      – SubjectFull: Brown algae
        Type: general
      – SubjectFull: Microbial polysaccharides
        Type: general
      – SubjectFull: Enzyme specificity
        Type: general
      – SubjectFull: Saccharina
        Type: general
      – SubjectFull: Polysaccharides
        Type: general
    Titles:
      – TitleFull: Biochemical characterization of mannuronan C5-epimerase from Saccharina japonica.
        Type: main
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          Name:
            NameFull: Meng, Xue
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            NameFull: Li, Shuang
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            NameFull: Zhang, Jie
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            NameFull: Duan, Delin
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            – D: 01
              M: 05
              Text: May2026
              Type: published
              Y: 2026
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              Value: 20965508
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              Value: 44
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            – TitleFull: Journal of Oceanology & Limnology
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