LAUSR

Abstract Inorganic materials exhibiting layered structures have recently been progressively utilised in biomedical fields. Among them, zirconium phosphate (ZrP) displays various unique layered structures. Thus, ZrP particles have been employed as an attractive alternative for numerous applications. In the current article, the synthesis of ZrP particles as new protein adsorbents and enzyme immobilising materials is explored. The effects of ZrP as enzyme immobilising agents have not been previously characterised. The materials were prepared under mild conditions and exhibited excellent enzyme adsorption abilities and remarkable catalytic activity. It was revealed that both the enzyme conformations and the carrier structures were modified following immobilisation. It was also supposed that only the mesopores in the prepared ZrP were used for the enzyme immobilisation. Additionally, the enhancement of the catalytic activity of the enzyme after immobilisation on ZrP was explained based on the changes of its three-dimensional structures. The electrochemical properties analysis showed that the enzyme immobilised on ZrP displayed outstanding sensitivity for hydrogen peroxide. According these results, ZrP is expected to be implemented in enzyme electrodes at low substrate concentrations. It is thought that the results presented in the current study on the properties of ZrP will have a significant impact in the fields of bioseparation and biosensing.