Matter‐tag: A universal immobilization platform for enzymes on polymers, metals, and silicon‐based materials

Enzyme immobilization is extensively studied to improve enzyme properties in catalysis and analytical applications. Here, we introduce a simple and versatile enzyme immobilization platform based on adhesion‐promoting peptides, namely Matter‐tags. Matter‐tags immobilize enzymes in an oriented way as a dense monolayer. The immobilization platform was established with three adhesion‐ promoting peptides; Cecropin A (CecA), liquid chromatography peak I (LCI), and Tachystatin A2 (TA2), that were genetically fused to enhanced green fluorescent protein and to two industrially important enzymes: a phytase (from Yersinia mollaretii) and a cellulase (CelA2 from a metagenomic library). Here, we report a universal and simple Matter‐tag–based immobilization platform for enzymes on various materials including polymers (polystyrene, polypropylene, and polyethylene terephthalate), metals (stainless steel and gold), and silicon‐based materials (silicon wafer). The Matter‐tag–based enzyme immobilization is performed at ambient temperature within minutes (<10 min) in an aqueous solution harboring the phytase or cellulase by immersing the targeted material. The peptide LCI was identified as universal adhesion promoter; LCI immobilized both enzymes on all investigated materials. The attachment of phytase‐LCI onto gold was characterized with surface plasmon resonance spectroscopy obtaining a dissociation constant value (KD) of 2.9·10−8 M and a maximal surface coverage of 504 ng/cm².

Publication year: 2019
Authors: Sarah Dedisch 1,2 Annika Wiens 2 Mehdi D. Davari 2 Dominik Söder 1 Cesar Rodriguez‐Emmenegger 1,3 Felix Jakob 1,2 Ulrich Schwaneberg 1,2

1 DWI–Leibniz‐Institute for InteractiveMaterials, Aachen, Germany

2 Lehrstuhl für Biotechnologie, RWTH AachenUniversity, Aachen, Germany

3 Institute of Technical and MacromolecularChemistry, RWTH Aachen University, Aachen,Germany

Published in: Biotechnology and Bioengineerging
DOI: 10.1002/bit.27181


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