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Catalysts 2019, 9(4), 354;

Site-Specific Addressing of Particles and Coatings via Enzyme-Mediated Destabilization

Department of Chemistry–Biobased and Bioinspired Materials, Paderborn University, Warburger Street 100, 33098 Paderborn, Germany
Author to whom correspondence should be addressed.
Received: 4 March 2019 / Revised: 1 April 2019 / Accepted: 10 April 2019 / Published: 12 April 2019
PDF [5525 KB, uploaded 12 April 2019]


Enzyme mediated addressing (EMA) is a highly specific and easy-to-apply technology for direction and deposition of particles and coatings on surfaces. Key feature of this process is an enzymatic reaction in direct proximity to the surface, which induces the deposition. The technique has previously shown great success in the handling of biological particles. In this study, addressing of non-biological nanoparticles, in particular plastics and metals, is presented. The respective particles are stabilized by an amphiphilic, enzyme-degradable block copolymer, consisting of poly(ethylene glycol) and poly(caprolactone). After contact with the enzyme pseudomonas lipase, the particles are destabilized, due to the loss of the hydrophilic part of the block copolymer. The lipase is therefore immobilized on glass supports. Immobilization is performed via adsorption or covalent bonding to epoxide groups. All deposition experiments show that addressing of individual particles occurs precisely within the predefined areas of enzyme activity. Depending on the material and reaction conditions, intact nanoparticles or coatings from such can be gained. The quintessence of the study is the indifference of the EMA regarding particle materials. From this rationale, the technique offers near unlimited materials compatibility within a precise, easy-to-apply, and upscalable process. View Full-Text
Keywords: enzymes; immobilization; nanoparticles; coatings; pseudomonas lipase enzymes; immobilization; nanoparticles; coatings; pseudomonas lipase

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Wedegärtner, D.; Strube, O.I. Site-Specific Addressing of Particles and Coatings via Enzyme-Mediated Destabilization. Catalysts 2019, 9, 354.

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