Co-immobilization of 8-xylosidase and endoxylanase on zirconium based metal-organic frameworks for improving xylosidase activity at high temperature and in acetone

作者：Li, Na; Xia, Huan; Jiang, Yanbin^*; Xiong, Jun; Lou, Wenyong

来源：Bioresource Technology, 2023, 383: 129240.

DOI：10.1016/j.biortech.2023.129240

• 8-Xylosidase
• Co-immobilization
• High temperature
• Acetone
• Metal-organic framework

Improving the activity of 8-xylosidase at high temperature and organic solvents is important for the conversion of xylan, phytochemicals and some hydroxyl-containing substances to produce xylose and bioactive substances. In this study, a 8-xylosidase R333H and an endoxylanase were simultaneously co-immobilized on the metal-organic framework UiO-66-NH2. Compared with the single R333H immobilization system, the co-immobilization enhanced the activity of R333H at high temperature and high concentration of acetone, and the relative ac-tivities at 95 degrees C and 50% acetone solution were >95%. The Km value of co-immobilized R333H towards p-Nitrophenyl-8-D-xylopyranoside (pNPX) shifted from 2.04 to 0.94 mM, which indicated the enhanced affinity towards pNPX. After 5 cycles, the relative activities of the co-immobilized enzymes towards pNPX and corncob xylan were 52% and 70% respectively, and the accumulated amount of reducing sugars obtained by co -immobilized enzymes degrading corncob xylan in 30% (v/v) acetone solution was 1.7 times than that with no acetone.

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  茂名学院