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- W2480702178 abstract "Nanoparticles (NPs) based on the complexation of anionic poly(maleic acid-co-propylene) (PMAP) and cationic poly(ethyleneimine) (PEI) are introduced as novel strategy to immobilize pollutant removing enzymes under mild, aqueous, and nontoxic conditions, in few processing steps. PEI/PMAP NP size 80–230 nm and are colloidally stable. Dried PEI/PMAP NP at model substrates remain bound after water contact if molar mixing ratio between cationic and anionic groups is close to unity. This study claims deswelling by drying, hydrophobic nature, and merging of PEI/PMAP NP as prime factors for adhesive stability. Furthermore PEI/PMAP NPs bear uncomplexed free maleic acid groups of PMAP, which react to maleic anhydride groups above 100 °C. These maleic anhydride groups can be used for both additional intraparticle crosslinking of PEI/PMAP NP and intermolecular linkage of enzymes under formation of imide or amide chemical bonds. Herein, laccase is either bound to precasted binary PEI/PMAP NP films or integrated into casted ternary laccase/PEI/PMAP NP films. Bound or integrated laccase shows significant enzymatic activity toward model pollutant guaiacol. Laccase bound by electrostatic attraction shows slightly higher enzymatic activity compared to chemical linkage at PEI/PMAP NP films. After five consecutive cycles of guaiacol conversion above laccase/PEI/PMAP NP film activity remains dropping to 30% of initial value." @default.
- W2480702178 created "2016-08-23" @default.
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- W2480702178 date "2016-08-03" @default.
- W2480702178 modified "2023-10-03" @default.
- W2480702178 title "Adhesive Reactive Nanoparticles of Poly(ethyleneimine)/Poly(maleic acid-co -propylene) Complexes: A Novel Concept for the Immobilization of Pollutant Removing Laccase" @default.
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- W2480702178 doi "https://doi.org/10.1002/macp.201600247" @default.
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