دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: Functional Characterization of a New GH107 Endo-α-(1,4)-Fucoidanase from the Marine Bacterium Formosa haliotis .
المؤلفون: Vuillemin M; Protein Chemistry and Enzyme Technology Section, DTU Bioengineering, Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark., Silchenko AS; 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., Cao HTT; NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, 02 Hung Vuong Street, Nhatrang 650000, Vietnam., Kokoulin MS; 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., Trang VTD; Protein Chemistry and Enzyme Technology Section, DTU Bioengineering, Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.; NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, 02 Hung Vuong Street, Nhatrang 650000, Vietnam., Holck J; Protein Chemistry and Enzyme Technology Section, DTU Bioengineering, Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark., Ermakova SP; 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., Meyer AS; Protein Chemistry and Enzyme Technology Section, DTU Bioengineering, Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark., Mikkelsen MD; Protein Chemistry and Enzyme Technology Section, DTU Bioengineering, Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
المصدر: Marine drugs [Mar Drugs] 2020 Nov 17; Vol. 18 (11). Date of Electronic Publication: 2020 Nov 17.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101213729 Publication Model: Electronic Cited Medium: Internet ISSN: 1660-3397 (Electronic) Linking ISSN: 16603397 NLM ISO Abbreviation: Mar Drugs Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, [2003]-
مواضيع طبية MeSH: Bacterial Proteins/*metabolism , Flavobacteriaceae/*enzymology , Glycoside Hydrolases/*metabolism , Polysaccharides/*metabolism, Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/isolation & purification ; Cloning, Molecular ; Enzyme Stability ; Flavobacteriaceae/genetics ; Glycoside Hydrolases/genetics ; Glycoside Hydrolases/isolation & purification ; Hydrogen-Ion Concentration ; Hydrolysis ; Sodium Chloride/chemistry ; Substrate Specificity ; Temperature
مستخلص: 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 Ca 2+ , Mn 2+ , Zn 2+ or Ni 2+ , for maximal activity. This new enzyme has the potential to serve the need for controlled enzymatic fucoidan depolymerization to produce bioactive sulfated fucoidan oligomers.
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معلومات مُعتمدة: 720755 European Commission H2020 Bio-based Industries Joint Consortium via the Macro Cascade Project; ĐTĐL.CN-57/19 Ministry of Science and Technology of Vietnam; x Technical University of Denmark and the FucoSan Program, Health from the Sea Project, supported by EU InterReg-Deutschland-Denmark and the European Fund of Regional Development
فهرسة مساهمة: Keywords: Fucus evanescens; GH107; fuco-oligosaccharides; fucoidan; fucoidanase
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Polysaccharides)
451W47IQ8X (Sodium Chloride)
9072-19-9 (fucoidan)
EC 3.2.1.- (Glycoside Hydrolases)
SCR Organism: Formosa haliotis
تواريخ الأحداث: Date Created: 20201120 Date Completed: 20210518 Latest Revision: 20240330
رمز التحديث: 20240330
مُعرف محوري في PubMed: PMC7698502
DOI: 10.3390/md18110562
PMID: 33213084
قاعدة البيانات: MEDLINE
الوصف
تدمد:1660-3397
DOI:10.3390/md18110562