Polyamide-based supports for multi-enzyme bio-catalysis

• Author(s): Braz, Joana Filipa Barros ; Dencheva, Nadya Vasileva ; Denchev, Z.
• Date: 2024
• Persistent ID: https://hdl.handle.net/1822/94169
• Origin: RepositóriUM - Universidade do Minho
• Document Type: Conference poster
• Language: English
• Contributor(s): Universidade do Minho

Description

Polyamide-Based Supports for Multi-Enzyme Biocatalysis Joana Barros Braz*1, Nadya Vasileva Dencheva1 and Zlatan Zlatev Denchev1 1: IPC – Institute for Polymers and Composites, University of Minho, Guimarães, Portugal *Presenting author: [e-mail] Abstract text: 250 words max. Enzymatic catalytic processes are known to be much more effective and environmentally friendly as compared to most conventional chemical catalytic methods. In nature, the more complex biocatalytic processes often require several enzymes to act simultaneously or consecutively. As an attempt to study and mimic this reaction path in industry, research has shifted towards multienzyme biocatalytic systems, since they permit complex processes to be performed as in one-pot reactions. This approach eliminates the need for separating intermediate products, reduces waste generation, and shortens reaction times [1]. Despite the many benefits that enzymes offer when used in their free form, their application in large-scale industrial processes has not reached its full potential. This is due to their instability under unfavourable operating conditions, their limited shelf-life, and the difficulties in recycling and recovering them. Enzyme immobilization on appropriate supports can often overcome these challenges [2]. The major challenge in making multi-enzyme supports is controlling the relative position of the enzymes in a limited space, reducing the distance between the enzyme molecules, decreasing the transfer distance of intermediate products, and improving catalytic efficiency. In this work, highly porous polyamide (PA) microparticles based on PA4, PA6, PA12, and the 1:1 by mol co-polymer PA12/6 are tested as supports for bi-enzyme immobilization. The enzyme pair horseradish peroxidase and glucose oxidase were immobilized sequentially and randomly onto the polyamide supports. Their catalytic efficiency and kinetic parameters were assessed in the cascade reaction for glucose detection. References [1] Z. Tan, H. Cheng, G. Chen, F. Ju, J. Fernández-Lucas, J. Zdarta, T. Jesionowski, M. Bilal Int. J. Biol. Macromol. 2023, vol 227, 535-550. [2] A. Basso, A. Serban, Mol. Catal. 2019, vol 479, 110607