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Article

Functional Characterization of a New GH107 Endo-α-(1,4)-Fucoidanase from the Marine Bacterium Formosa haliotis

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Protein Chemistry and Enzyme Technology Section, DTU Bioengineering, Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark
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NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, 02 Hung Vuong Street, Nhatrang 650000, Vietnam
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G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 159, Prospect 100-let Vladivostoku, 690022 Vladivostok, Russia
*
Author to whom correspondence should be addressed.
Mar. Drugs 2020, 18(11), 562; https://doi.org/10.3390/md18110562
Received: 19 October 2020 / Revised: 5 November 2020 / Accepted: 11 November 2020 / Published: 17 November 2020
Fucoidans from brown macroalgae are sulfated fucose-rich polysaccharides, that have several beneficial biological activities, including anti-inflammatory and anti-tumor effects. Controlled enzymatic depolymerization of the fucoidan backbone can help produce homogeneous, defined fucoidan products for structure-function research and pharmaceutical uses. However, only a few endo-fucoidanases have been described. This article reports the genome-based discovery, recombinant expression in Escherichia coli, stabilization, and functional characterization of a new bacterial endo-α-(1,4)-fucoidanase, Fhf1, from Formosa haliotis. Fhf1 catalyzes the cleavage of α-(1,4)-glycosidic linkages in fucoidans built of alternating α-(1,3)-/α-(1,4)-linked l-fucopyranosyl sulfated at C2. The native Fhf1 is 1120 amino acids long and belongs to glycoside hydrolase (GH) family 107. Deletion of the signal peptide and a 470 amino acid long C-terminal stretch led to the recombinant expression of a robust, minimized enzyme, Fhf1Δ470 (71 kDa). Fhf1Δ470 has optimal activity at pH 8, 37–40 °C, can tolerate up to 500 mM NaCl, and requires the presence of divalent cations, either Ca2+, Mn2+, Zn2+ or Ni2+, for maximal activity. This new enzyme has the potential to serve the need for controlled enzymatic fucoidan depolymerization to produce bioactive sulfated fucoidan oligomers. View Full-Text
Keywords: fucoidan; fucoidanase; Fucus evanescens; GH107; fuco-oligosaccharides fucoidan; fucoidanase; Fucus evanescens; GH107; fuco-oligosaccharides
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MDPI and ACS Style

Vuillemin, M.; Silchenko, A.S.; Cao, H.T.T.; Kokoulin, M.S.; Trang, V.T.D.; Holck, J.; Ermakova, S.P.; Meyer, A.S.; Mikkelsen, M.D. Functional Characterization of a New GH107 Endo-α-(1,4)-Fucoidanase from the Marine Bacterium Formosa haliotis. Mar. Drugs 2020, 18, 562. https://doi.org/10.3390/md18110562

AMA Style

Vuillemin M, Silchenko AS, Cao HTT, Kokoulin MS, Trang VTD, Holck J, Ermakova SP, Meyer AS, Mikkelsen MD. Functional Characterization of a New GH107 Endo-α-(1,4)-Fucoidanase from the Marine Bacterium Formosa haliotis. Marine Drugs. 2020; 18(11):562. https://doi.org/10.3390/md18110562

Chicago/Turabian Style

Vuillemin, Marlene, Artem S. Silchenko, Hang T.T. Cao, Maxim S. Kokoulin, Vo T.D. Trang, Jesper Holck, Svetlana P. Ermakova, Anne S. Meyer, and Maria D. Mikkelsen. 2020. "Functional Characterization of a New GH107 Endo-α-(1,4)-Fucoidanase from the Marine Bacterium Formosa haliotis" Marine Drugs 18, no. 11: 562. https://doi.org/10.3390/md18110562

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