Immobilization of mushroom polyphenol oxidase on poly(allyl glycidyl ether-co-ethylene glycol dimethacrylate) macroporous beaded copolymers

Vaidya, Bhalchandra K.; Karale, Abhijeet J.; Suthar, Hitesh K.; Ingavle, Ganesh; Pathak, Tara Sankar; Ponrathnam, S.; Nene, Sanjay

doi:10.1016/j.reactfunctpolym.2007.05.015

Cited by 11 publications

(1 citation statement)

References 26 publications

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“…23 Thus, a different approach is taken here, in which a glycidyl methacryate-containing copolymer, which is well known to react with amino groups, is used to provide a point of attachment for proteins. [24][25][26][27] This copolymer membrane supports both focused ion beam (FIB) milling and one-step immobilization of the enzyme. These structures are used to study the turnover of horseradish peroxidase (HRP) on the planar surfaces of microfluidic channels.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic activity of surface-immobilized horseradish peroxidase confined to micrometer- to nanometer-scale structures in nanocapillary array membranes

Wang

King

Branagan

et al. 2009

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Horseradish peroxidase (HRP) was immobilized on the planar surfaces and inside the cylindrical nanopores of nanocapillary array membranes (NCAMs) to study how the enzyme-catalyzed oxidation of a fluorigenic substrate, Amplex Red (AR), to fluorescent resorufin by hydrogen peroxide is influenced by confinement. Because AR was also found to be converted to resorufin photolytically at high laser fluences, a modified laser-induced fluorescence protocol was developed to characterize the enzyme-catalyzed reaction in the absence of interference from the photolytic reaction. Surface-immobilized HRP was studied in two environments: bound to the surface of a microfluidic channel, and bound to the interior of cylindrical nanopores in NCAMs connecting crossed microfluidic channels. HRP was immobilized through reaction of solvent-accessible primary amines with the epoxy group of the methyl methacrylate-glycidyl methacrylate copolymer synthesized in either planar or annular geometries to construct the test structures for enzymatic activity. HRP immobilized on planar surfaces shows high activity (approximately 10 microM min(-1)) meaning that the copolymer membrane exhibits good potential for immobilizing the enzyme, especially since active structures are obtained in a one-step reaction. HRP was also immobilized inside nanopores via physisorption. Enzymatic reactions inside the nanopores were characterized and compared to finite element simulations of a modified Eley-Rideal mechanism to bracket the value of the overall rate constant for the confined enzyme. Reaction velocities were estimated to be approximately 10-fold higher in the nanopores than for the same enzyme bound to a planar microfluidic surface.

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Section: Introductionmentioning

confidence: 99%

Enzymatic activity of surface-immobilized horseradish peroxidase confined to micrometer- to nanometer-scale structures in nanocapillary array membranes

Wang

King

Branagan

et al. 2009

Analyst

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Immobilization of Candida lipolytica lipase on macroporous beaded terpolymers with epoxy groups

Li¹,

Duan²,

Meng³

et al. 2012

J of Applied Polymer Sci

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A series of macroporous beaded terpolymers with epoxy groups were synthesized by suspension polymerization with glycidyl methacrylate (GMA), ethylene glycol dimethacrylate (EGDMA), and the third monomers including styrene, methyl methacrylate, n-butyl acrylate (BA), butyl methacrylate (BMA), and 2-hydroxyethyl methacrylate for immobilization of Candida lipolytica lipase. The effect of various third monomers on loading and activity recovery of immobilized lipase were studied. Terpolymers with BA as the third monomer were found to give the biggest loading of lipase, and the activity recovery of lipase immobilized on poly (GMA-EGDMA-BA) terpolymers reached 79.0%. As the content of BA (%) increasing, the loading of lipase enhanced, but the activity recovery reached 88.5% for the initial stage and decreased to 46.9% at last. The poly(GMA-EGDMA-BA-10) showed an optimal result in lipase immobilization. Lipase immobilized on poly(GMA-EGDMA-BA-10) carriers had broader pH and higher temperature stability.

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Effect of the surface parameters on the interaction of epoxy polymer supports with a lipase enzyme

et al. 2014

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Immobilization of mushroom polyphenol oxidase on poly(allyl glycidyl ether-co-ethylene glycol dimethacrylate) macroporous beaded copolymers

Cited by 11 publications

References 26 publications

Enzymatic activity of surface-immobilized horseradish peroxidase confined to micrometer- to nanometer-scale structures in nanocapillary array membranes

Enzymatic activity of surface-immobilized horseradish peroxidase confined to micrometer- to nanometer-scale structures in nanocapillary array membranes

Immobilization of Candida lipolytica lipase on macroporous beaded terpolymers with epoxy groups

Effect of the surface parameters on the interaction of epoxy polymer supports with a lipase enzyme

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