Journal
SEPARATION AND PURIFICATION TECHNOLOGY
Volume 297, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.seppur.2022.121505
Keywords
Immobilized enzyme; Mesoporous nanocarriers; Metal-organic frameworks
Categories
Funding
- National Natural Science Foundation of China [21878131, 22078133, U1904174]
- Opening Project of Henan Province Key Laboratory of Water Pollution Control and Rehabilitation Technology [CJSZ2021002, CJSP2021001]
Ask authors/readers for more resources
Metal-organic frameworks (MOFs) with adjustable mesopores were prepared through bionic mineralization using protein as a template. The study found that UIO-66 with a pore size of 6.46 nm exhibited the highest loading capacities for the investigated enzymes, and the immobilized enzymes showed improved stability and substrate affinity compared to the free enzymes.
A metal-organic frameworks (MOFs) with adjustable mesopores was prepared through bionic mineralization using protein as template in this paper. By regulating the content of bovine serum, pore structures of different sizes (6.46, 7.55, 10.80 nm) were obtained, used for the immobilization of enzymes (HRP, laccase and cellulase). It was found that the UIO-66 with a pore size of 6.46 nm exhibited the highest loading capacities for the investigated three enzymes. Under optimized conditions for immobilization, the maximum loading capacity of HRP, laccase and cellulase was 205.7, 214.2 and 203.9 mg g-1, respectively. It should be noted that the stabilities of the three immobilized HRP@UIO-66, laccase@UIO-66 and cellulase@UIO-66 were significantly improved due to the favorable fitting between the pore size of the carrier material and the enzyme molecular size. In particular, the substrate affinity of the immobilized HRP@UIO-66 (0.120 g L-1) is similar to that of free HRP (0.122 g L-1). It is mainly due to that the appropriate porous structure of the carrier could avoid the obstruction of the substrate mass transfer channel after the adsorption of enzyme molecules. Moreover, the porous structure has a certain enrichment effect on the substrate, which promotes the catalytic efficiency of immobilized enzymes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available