Modification of native fucoidan from Fucus evanescens by recombinant fucoidanase from marine bacteria Formosa algae

Carbohydr Polym. 2018 Aug 1:193:189-195. doi: 10.1016/j.carbpol.2018.03.094. Epub 2018 Mar 30.

Abstract

Enzymatic depolymerization of fucoidans attracts many researchers due to the opportunity of obtaining standardized fucoidan fragments. Fucoidanase catalyzes the cleavage of fucoidan from Fucus evanescens (FeF) to form low molecular weight products (LMP) and a polymeric fraction (HMP) with 50.8 kDa molecular weight and more than 50% yield. NMR spectroscopy shows that the HMP fraction has regular structure and consists of a repeating fragment [→3)-α-l-Fucp2,4OSO3--(1 → 4)-α-l-Fucp2,4OSO3--(1 → 4)-α-l-Fucp2OSO3--(1→]n. The anticancer effects of FeF fucoidan and its derivative (HMP) were studied in vitro on colon cancer cells HCT-116, HT-29, and DLD-1. The anticancer activity of the HMP fraction was found to be slightly lower than that of the FeF fucoidan. Research and practical applications of the enzyme include modification of native fucoidans for purposes of regular and easier characterized derivatives acquisition.

Keywords: Anticancer activity; Endo-fucoidanase; Fucoidan depolymerization; Fucoidan from Fucus evanescens; Fucoidanase; Marine bacteria.

MeSH terms

  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / metabolism
  • Antineoplastic Agents / pharmacology*
  • Biocatalysis
  • Carbohydrate Conformation
  • Cell Proliferation / drug effects
  • Dose-Response Relationship, Drug
  • Drug Screening Assays, Antitumor
  • Fucus / chemistry*
  • Fucus / enzymology*
  • Fucus / metabolism
  • Humans
  • Hydrolases / chemistry
  • Hydrolases / metabolism*
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism
  • Polysaccharides / pharmacology*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship
  • Tumor Cells, Cultured

Substances

  • Antineoplastic Agents
  • Polysaccharides
  • Recombinant Proteins
  • fucoidan
  • Hydrolases