Abstract

Immobilization is a method for making an enzyme more robust in the environment, especially in terms of its stability and reusability. A mutant phosphotriesterase (YT PTE) isolated from Pseudomonas dimunita has been reported to have high proficiency in hydrolyzing the Sp and Rp-enantiomers of organophosphate chromophoric analogs and therefore has great potential as a decontamination agent and biosensor. This work aims to investigate the feasibility of using Fuller’s earth (FE) as a YT PTE immobilization support and characterize its biochemical features after immobilization. The immobilized YT PTE was found to show improvement in thermal stability with a half-life of 24 h compared to that of the free enzyme, which was only 8 h. The stability of the immobilized YT PTE allowed storage for up to 4 months and reuse for up to 6 times. The immobilized YT PTE showed high tolerance against all tested metal ions, Tween 40 and 80 surfactants and inorganic solvents. These findings showed that the immobilized YT PTE became more robust for use especially with regards to its stability and reusability. These features would enhance the future applicability of this enzyme as a decontamination agent and its use in other suitable industrial applications.

Highlights

  • Published: 17 August 2021The application of enzymes in various processes, especially in the food, pharmaceutical, detergent and biosensing industries has gained much interest in recent times [1].the stability of these enzymes in the environments that they are used in or when used under harsh usage conditions continues to be a matter of concern [2]

  • The utilization of PTE as a means to inactivate organophosphate esters (OP) is an application that could address concerns about their use and subsequent inactivation after use in these industries. The immobilization of this enzyme onto a support could provide a means for its wider use, a need that has become a matter of great interest due to PTE’s wide potential application and in view of the current high costs of cleaning up environmental contamination from the residues of OP use

  • We report on the successful immobilization of YT PTE onto Fuller’s earth (FE) using the physical adsorption method

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Summary

Introduction

Published: 17 August 2021The application of enzymes in various processes, especially in the food, pharmaceutical, detergent and biosensing industries has gained much interest in recent times [1].the stability of these enzymes in the environments that they are used in or when used under harsh usage conditions continues to be a matter of concern [2]. Phospotriesterase (PTE) is an enzyme that is known to be able to hydrolyze toxic organophosphate esters (OP) into non-toxic compounds [3,4] This toxic functionality is widely present in various industries such as in agriculture, petroleum, plasticizer production, textile manufacturing and they have been used as chemical warfare agents [5,6]. The utilization of PTE as a means to inactivate OPs is an application that could address concerns about their use and subsequent inactivation after use in these industries The immobilization of this enzyme onto a support could provide a means for its wider use, a need that has become a matter of great interest due to PTE’s wide potential application and in view of the current high costs of cleaning up environmental contamination from the residues of OP use. Most of this work was for the purpose of detecting the presence of OPs and was only in Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations

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