Issue 14, 2022

Development of polymer-based multifunctional composite particles of protease and peroxidase activities

Abstract

A hybrid material (SL–PPN–HEP–HRP) of dual enzyme function was prepared by co-immobilization of papain (PPN) and horseradish peroxidase (HRP) on sulphate latex (SL) microspheres using heparin (HEP) polyelectrolyte as a building block in the sequential adsorption method. The doses of PPN, HEP and HRP were optimized in each step of the preparation process to achieve high functional and colloidal stability. The enzymes and the polyelectrolyte strongly adsorbed on the oppositely charged surfaces via electrostatic forces, and enzyme leakage was not observed from the hybrid material, as confirmed by colorimetric protein tests and microscopy measurements. It was found that the polyelectrolyte acted as a separator between PPN and HRP to prevent hydrolytic attack on the latter enzyme, which otherwise prevents the joint use of these important biocatalysts. Excellent colloidal stability was obtained for the SL–PPN–HEP–HRP composite and the embedded PPN and HRP showed remarkable protease and peroxidase activities, respectively, at least until five days after preparation. The present results offer a promising approach to develop biocatalytic systems of dual function, which are often required in manufacturing processes in the food industry, where the colloidal stability of such multifunctional materials is a key parameter to achieve remarkable efficiency.

Graphical abstract: Development of polymer-based multifunctional composite particles of protease and peroxidase activities

Supplementary files

Article information

Article type
Paper
Submitted
26 Aug. 2021
Accepted
27 Okt. 2021
First published
27 Okt. 2021
This article is Open Access
Creative Commons BY license

J. Mater. Chem. B, 2022,10, 2523-2533

Development of polymer-based multifunctional composite particles of protease and peroxidase activities

S. Sáringer, T. Valtner, Á. Varga, J. Maléth and I. Szilágyi, J. Mater. Chem. B, 2022, 10, 2523 DOI: 10.1039/D1TB01861B

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