z-logo
Premium
Matter‐ tag : A universal immobilization platform for enzymes on polymers, metals, and silicon‐based materials
Author(s) -
Dedisch Sarah,
Wiens Annika,
Davari Mehdi D.,
Söder Dominik,
RodriguezEmmenegger Cesar,
Jakob Felix,
Schwaneberg Ulrich
Publication year - 2020
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.27181
Subject(s) - cellulase , polystyrene , polymer , chemistry , smart polymer , immobilized enzyme , monolayer , biosensor , surface plasmon resonance , materials science , surface modification , enzyme , chemical engineering , nanotechnology , biochemistry , organic chemistry , nanoparticle , engineering
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 ( K D ) of 2.9·10 −8  M and a maximal surface coverage of 504 ng/cm².

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here