期刊
BIOTECHNOLOGY AND BIOENGINEERING
卷 117, 期 1, 页码 49-61出版社
WILEY
DOI: 10.1002/bit.27181
关键词
adhesion promoter; anchor peptides; immobilization; material binding peptides; surface functionalization
资金
- federal state of North Rhine-Westphalia [EFRE 30 00 883 02]
- Bundesministerium fur Bildung und Forschung [031B0104B]
- EU
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 center dot 10(-8) M and a maximal surface coverage of 504 ng/cm(2).
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