Enzyme immobilization has been accepted as an efficient technique for improving the stability and recyclability of enzymes. Herein

biomimetic mineralization strategy was employed to achieve the immobilization of urease in a type of metal-organic frameworks (zeolite imidazolate framework-8

ZIF-8)

and the immobilized enzyme urease@ZIF-8 was systematically evaluated for its structure

activity

stability and recyclability

using the hydrolysis of urea as a model. The entrapment of urease was found to be realized in a synchronous manner with the formation of ZIF-8 crystal. The loading of urease in ZIF-8 was measured to be

ca

. 10.6% through the bicinchoninic acid (BCA) protein assay. The encapsulated urease could efficiently maintain its native conformation

which endowed the immobilized urease with excellent activity and stability

even in harsh conditions (

e.g

.

in the presence of trypsin

acidic or alkali conditions

or at high temperature). Further

urease@ ZIF-8 exhibited good recyclability during the degradation of urea

in which it could keep 58.86% of initial activity after being used for 5 cycles. Thus

biomimetic mineralization could be poten

tially utilized as a promising method to prepare immobilized ureases with superior activity

stability and recyclability

thereby facilitating the construction of efficient catalysts for industrial biocatalysis and biosensing.