Utilizing heterologously overexpressed endo-1,3-fucanase to investigate the structure of sulfated fucan from sea cucumber (Holothuria hilla)

Guangning Chen, Long Yu, Yuying Zhang, Yaoguang Chang, Yanyan Liu, Jingjing Shen, Changhu Xue

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

Sea cucumber sulfated fucan (SC-FUC) attracted increasing interests in the recent decades. Endo-1,3-fucanase has been employed in the structural clarification and structure-function relationship investigations of SC-FUC. Nevertheless, the preparation of wild-type endo-1,3-fucanase is costly and time-consuming, which hinders its further utilization. In this study, a heterologously overexpressed endo-1,3-fucanase (FunA) was introduced into structural identification of SC-FUC. FunA was efficiently prepared within one day and utilized in the investigation of sulfated fucan from sea cucumber Holothuria hilla (Hh-FUC). By using enzymatic degradation, glycomics and NMR analysis, the major structure of Hh-FUC was identified to be composed of a tetrasaccharide repeating unit →3-α-L-Fucp-1 → 3-α-L-Fucp2,4(OSO3)-1 → 3-α-L-Fucp2(OSO3)-1 → 3-α-L-Fucp2(OSO3)-1→. Due to the efficient acquisition of enzyme and the superior oligosaccharide recovery, 0.6 mL of E. coli broth and 10 mg of Hh-FUC were sufficient for the structural identification. The results demonstrated the superiority of heterologously overexpressed fucanase over its wild-type enzyme in structural investigation of sulfated fucan.

Original languageEnglish
Article number118480
Number of pages6
JournalCarbohydrate Polymers
Volume272
Early online date24 Jul 2021
DOIs
Publication statusPublished - 15 Nov 2021
Externally publishedYes

Keywords

  • Endo-1,3-fucanase
  • GH168
  • Sea cucumber
  • Structure
  • Sulfated fucan

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