دورية أكاديمية
The Endo-α(1,4) Specific Fucoidanase Fhf2 From Formosa haliotis Releases Highly Sulfated Fucoidan Oligosaccharides.
| العنوان: | The Endo-α(1,4) Specific Fucoidanase Fhf2 From Formosa haliotis Releases Highly Sulfated Fucoidan Oligosaccharides. |
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| المؤلفون: | Trang VTD; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.; NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, Nha Trang, Vietnam., Mikkelsen MD; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Vuillemin M; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Meier S; Department of Chemistry, Technical University of Denmark, Kongens Lyngby, Denmark., Cao HTT; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.; NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, Nha Trang, Vietnam., Muschiol J; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.; Ocean EcoSystems Biology Unit, GEOMAR Helmholtz Centre for Ocean Research Kiel, Kiel, Germany., Perna V; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Nguyen TT; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.; NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, Nha Trang, Vietnam., Tran VHN; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.; NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, Nha Trang, Vietnam., Holck J; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Van TTT; NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, Nha Trang, Vietnam., Khanh HHN; NhaTrang Institute of Technology Research and Application, Vietnam Academy of Science and Technology, Nha Trang, Vietnam., Meyer AS; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark. |
| المصدر: | Frontiers in plant science [Front Plant Sci] 2022 Feb 02; Vol. 13, pp. 823668. Date of Electronic Publication: 2022 Feb 02 (Print Publication: 2022). |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Frontiers Research Foundation Country of Publication: Switzerland NLM ID: 101568200 Publication Model: eCollection Cited Medium: Print ISSN: 1664-462X (Print) Linking ISSN: 1664462X NLM ISO Abbreviation: Front Plant Sci Subsets: PubMed not MEDLINE |
| أسماء مطبوعة: | Original Publication: Lausanne : Frontiers Research Foundation, 2010- |
| مستخلص: | Fucoidanases are endo-fucoidanases (also known as endo-fucanases) that catalyze hydrolysis of α-glycosidic linkages in fucoidans, a family of sulfated fucose-rich polysaccharides primarily found in the cell walls of brown seaweeds. Fucoidanases are promising tools for producing bioactive fucoidan oligosaccharides for a range of biomedical applications. High sulfation degree has been linked to high bioactivity of fucoidans. In this study, a novel fucoidanase, Fhf2, was identified in the genome of the aerobic, Gram-negative marine bacterium Formosa haliotis . Fhf2 was found to share sequence similarity to known endo-α(1,4)-fucoidanases (EC 3.2.1.212) from glycoside hydrolase family 107. A C-terminal deletion mutant Fhf2∆484, devoid of 484 amino acids at the C-terminus, with a molecular weight of approximately 46 kDa, was constructed and found to be more stable than the full-length Fhf2 protein. Fhf2∆484 showed endo-fucoidanase activity on fucoidans from different seaweed species including Fucus evanescens , Fucus vesiculosus , Sargassum mcclurei , and Sargassum polycystum . The highest activity was observed on fucoidan from F. evanescens . The Fhf2∆484 enzyme was active at 20-45°C and at pH 6-9 and had optimal activity at 37°C and pH 8. Additionally, Fhf2∆484 was found to be calcium-dependent. NMR analysis showed that Fhf2∆484 catalyzed hydrolysis of α(1,4) linkages between L-fucosyl moieties sulfated on C2 (similar to Fhf1 from Formosa haliotis ), but Fhf2∆484 in addition released oligosaccharides containing a substantial amount of 2,4-disulfated fucose residues. The data thus suggest that the Fhf2∆484 enzyme could be a valuable candidate for producing highly sulfated oligosaccharides applicable for fucoidan bioactivity investigations. Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. (Copyright © 2022 Trang, Mikkelsen, Vuillemin, Meier, Cao, Muschiol, Perna, Nguyen, Tran, Holck, Van, Khanh and Meyer.) |
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| فهرسة مساهمة: | Keywords: FTIR; Fucus evanescens; Sargassum mcclurei; T9SS; calcium dependency; sulfation |
| تواريخ الأحداث: | Date Created: 20220221 Latest Revision: 20220223 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC8847386 |
| DOI: | 10.3389/fpls.2022.823668 |
| PMID: | 35185990 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1664-462X |
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| DOI: | 10.3389/fpls.2022.823668 |