Immobilization β-glucosidase from Dictyoglomus thermophilum on UiO-66-NH 2 : An efficient catalyst for enzymatic synthesis of kinsenoside via reverse hydrolysis reaction.

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  • Author(s): Yuan X;Yuan X; Liao JH; Liao JH; Du GJ; Du GJ; Hou Y; Hou Y; Hu SQ; Hu SQ
  • Source:
    International journal of biological macromolecules [Int J Biol Macromol] 2024 Dec; Vol. 282 (Pt 5), pp. 137330. Date of Electronic Publication: 2024 Nov 06.
  • Publication Type:
    Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
    • Publication Information:
      Publication: Amsterdam : Elsevier
      Original Publication: Guildford, Eng., IPC Science and Technology Press.
    • Subject Terms:
      beta-Glucosidase*/metabolism ; beta-Glucosidase*/chemistry ; Enzymes, Immobilized*/chemistry ; Enzymes, Immobilized*/metabolism; Hydrolysis ; Enzyme Stability ; Biocatalysis ; Hydrogen-Ion Concentration ; Temperature ; Catalysis
    • Abstract:
      Kinsenoside is a rare and valuable glycoside with extensive bioactivities. However, the enzymatic synthesis of kinsenoside has been a challenging task due to the limited enzyme toolbox and unsatisfactory yield. Herein, the β-glucosidase from Dictyoglomus thermophilum (DtBGL) was heterologously expressed, purified and enzymatically characterized. The purified DtBGL was successfully immobilized on the metal-organic frameworks of UiO-66-NH 2 . The DtBGL@UiO-66-NH 2 was fully characterized using SEM, XRD, TGA and FTIR. The studies on enzymatic properties demonstrated that DtBGL@UiO-66-NH 2 exhibited increased catalytic activity and stability compared to the free DtBGL. Particularly, DtBGL@UiO-66-NH 2 could catalyze the synthesis of kinsenoside via the reverse hydrolysis reaction and the kinsenoside yield was 34.12 % under the optimized catalytic system, which was 1.9-fold higher compared with the free DtBGL. Moreover, DtBGL@UiO-66-NH 2 displayed good reusability with a kinsenoside yield of 27.02 % after reuse for 3 times. The present work not only identifies and characterizes a highly active β-glucosidase with reverse hydrolysis activity, but also proposes the immobilized enzyme as an effective catalyst for the industrial production of glycosides.
      Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
      (Copyright © 2024 Elsevier B.V. All rights reserved.)
    • Contributed Indexing:
      Keywords: Immobilization; Reverse hydrolysis; β-Glucosidase
    • Accession Number:
      EC 3.2.1.21 (beta-Glucosidase)
      0 (Enzymes, Immobilized)
    • Publication Date:
      Date Created: 20241108 Date Completed: 20241203 Latest Revision: 20241203
    • Publication Date:
      20241204
    • Accession Number:
      10.1016/j.ijbiomac.2024.137330
    • Accession Number:
      39515718