Carrier Variety Used in Immobilization of His6-OPH Extends Its Application Areas

Abstract

Organophosphorus hydrolase, containing a genetically introduced hexahistidine sequence (His₆-OPH), attracts the attention of researchers by its promiscuous activity in hydrolytic reactions with various substrates, such as organophosphorus pesticides and chemical warfare agents, mycotoxins, and N-acyl homoserine lactones. The application of various carrier materials (metal-organic frameworks, polypeptides, bacterial cellulose, polyhydroxybutyrate, succinylated gelatin, etc.) for the immobilization and stabilization of His₆-OPH by various methods, enables creation of biocatalysts with various properties and potential uses, in particular, as antidotes, recognition elements of biosensors, in fibers with chemical and biological protection, dressings with antimicrobial properties, highly porous sorbents for the degradation of toxicants, including in flow systems, etc. The use of computer modeling methods in the development of immobilized His₆-OPH samples provides in silico prediction of emerging interactions between the enzyme and immobilizing polymer, which may have negative effects on the catalytic properties of the enzyme, and selection of the best options for experiments in vitro and in vivo. This review is aimed at analysis of known developments with immobilized His₆-OPH, which allows to recognize existing recent trends in this field of research, as well as to identify the reasons limiting the use of a number of polymer molecules for the immobilization of this enzyme.

Keywords: N-acyl homoserine lactones; biocatalysis; hexa-histidine tag; immobilization; mycotoxins; organophosphorus compounds; organophosphorus hydrolase; stabilization.

Figure 1

Various methods of immobilization (red) and applications (blue) of hexa-histidine-containing OPH.

Figure 2

Application of His₆-OPH in the content of EPC for the degradation of some mycotoxins in the content of animal feed and in the frame of protective fiber cover.