Polymer-Assisted Biocatalysis: Effects of Macromolecular Architectures on the Stability and Catalytic Activity of Immobilized Enzymes toward Water-Soluble and Water-Insoluble Substrates

ACS Omega
Dieter M Scheibel, Ivan Gitsov

Abstract

The aim of this study is to develop efficient enzyme immobilization media that will enable the reuse of the biocatalysts over multiple cycles, increase their thermal stability, and attenuate their activity toward hydrophobic substrates for "green" transformations in aqueous media. For this purpose, amphiphilic AB and ABA block copolymers were synthesized and tested with laccase (a multicopper oxidase). In all cases, the hydrophilic B block consisted of poly(ethylene glycol), PEG, with molecular masses of 3, 5, 13, 20, or 13 kDa poly(ethylene oxide). The hydrophobic A blocks were made of linear poly(styrene), PS; hyperbranched poly(p-chloromethyl styrene); or dendritic poly(benzyl ether)s of generations 2, 3, and 4 (G2, G3, and G4) with molecular masses ranging from 1 to 24 kDa. A total of 23 different copolymers (self-assembling into micelles or physical networks) were evaluated. Notable activity enhancements were achieved with both micelles (up to 253%) and hydrogels (up to 408%). The highest enzymatic activity and thermal stability were observed with laccase immobilized in hydrogels consisting of the linear ABA block copolymer PS2.7k-PEG3k-PS2.7k (13 290 μkat/L, 65 °C, ABTS test). This represents a 1245% improvement over nati...Continue Reading

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Methods Mentioned

BETA
dynamic light scattering
Scanning electron microscopy
Assay
NMR

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