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

• Published in: International journal of biological macromolecules 2024-12, Vol.282 (Pt 5), p.137330
• Main Authors: Yuan, Xin, Liao, Jia-Hui, Du, Gui-Jia, Hou, Yi, Hu, Song-Qing
• Format: Article
• Language: English
• Subjects: beta-Glucosidase - chemistry; beta-Glucosidase - metabolism; Biocatalysis; Catalysis; Enzyme Stability; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - metabolism; Hydrogen-Ion Concentration; Hydrolysis; Temperature
• ISSN: 1879-0003

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 . The DtBGL@UiO-66-NH was fully characterized using SEM, XRD, TGA and FTIR. The studies on enzymatic properties demonstrated that DtBGL@UiO-66-NH exhibited increased catalytic activity and stability compared to the free DtBGL. Particularly, DtBGL@UiO-66-NH 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 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.