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Immobilization of recombinant Escherichia coli whole cells harboring xylose reductase and glucose dehydrogenase for xylitol production from xylose mother liquor
- Jin, Li-Qun, Yang, Bo, Xu, Wei, Chen, Xian-Xiao, Jia, Dong-Xu, Liu, Zhi-Qiang, Zheng, Yu-Guo
- Bioresource technology 2019 v.285 pp. 121344
- Escherichia coli, cross-linking reagents, crosslinking, diatomaceous earth, enzymes, glucose, glutaraldehyde, half life, immobilized cells, raw materials, space and time, wastes, xylitol, xylose
- In this study, recombinant E. coli BL21(DE3)/pCDFDuet-1-XR-GDH harboring xylose reductase (XR) and glucose dehydrogenase (GDH) were immobilized and applied for the production of xylitol from xylose mother liquor (XML). Various immobilization methods were screened and the cross-linking approach with diatomite and polyetherimide as the raw materials and glutaraldehyde as the cross-linking agent was the optimal one, and the recovery activity reached of 80.3% after immobilization. The half-life of immobilized cells was 1.52 times to that of free cells. Batch experiments showed that the enzyme activity of immobilized cells remained 70.5% of the initial activity after 10 batches and the space-time yield of xylitol reached of 11.5 g/(L h). The production of xylitol from xylose mother liquor by immobilized E. coli cells containing xylose reductase and glucose dehydrogenase was reported for the first time, which paved a foundation for industrial production of xylitol from waste xylose mother liquor.