Covalent Enzyme Immobilization

Cao, Linqiu

doi:10.1002/3527607668.ch3

Cited by 8 publications

(1 citation statement)

References 81 publications

(110 reference statements)

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“…Polymers based on acrylonitrile can be prepared by polymerization of acrylonitrile or other unsaturated monomers bearing nitrile groups in the presence of comonomers such as acrylamide and a cross-linker, e.g. divinyl benzene or bisacrylamide (Ivanov and Yotova, 2002;Cao, 2006). In the same context, Boguslavsky et al (2005) have reported the preparations of polyacrylonitrile nanoparticles using dispersion/emulsion polymerization method (Boguslavsky et al, 2005).…”

Section: Introductionmentioning

confidence: 97%

Poly (acrylonitrile-co-methyl methacrylate) nanoparticles: I. Preparation and characterization

Eldin

El-Aassar

Elzatahry

et al. 2017

Arabian Journal of Chemistry

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This work concerns the preparation and characterization of poly (acrylonitrile-co-methyl methacrylate) Copolymer, P(AN-co-MMA), nano-particles using precipitation polymerization technique. Potassium per-sulfate redox initiation system was used to perform polymerization process in an alcoholic aqueous system. The impact of different polymerization conditions such as comonomer concentration and ratio, polymerization time, polymerization temperatures, initiator concentration and co-solvent composition on the polymerization yield and particle size was studied. Maximum polymerization yield, 70%, was obtained with MMA:AN (90%:10%) comonomer composition. Particle sizes ranging from 16 nm to 1483 nm were obtained and controlled by variation of polymerization conditions. The co-polymerization process was approved by FT-IR and TGA analysis. The copolymer composition was investigated by nitrogen content analysis. Copolymers with a progressive percentage of PAN show thermal stabilities close to PAN Homopolymer. SEM photographs prove spherical structure of the produced copolymers. The investigated system shows promising future in the preparation of nanoparticles from comonomers without using emulsifiers or dispersive agents. ª 2014 Production and hosting by Elsevier B.V. on behalf of King Saud University. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).

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Section: Introductionmentioning

confidence: 97%

Poly (acrylonitrile-co-methyl methacrylate) nanoparticles: I. Preparation and characterization

Eldin

El-Aassar

Elzatahry

et al. 2017

Arabian Journal of Chemistry

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Activation of immobilized lipase in non‐aqueous systems by hydrophobic poly‐DL‐tryptophan tethers

Schilke¹,

Kelly²

2008

Biotech & Bioengineering

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Many industrially important reactions use immobilized enzymes in non-aqueous, organic systems, particularly for the production of chiral compounds such as pharmaceutical precursors. The addition of a spacer molecule (“tether”) between a supporting surface and enzyme often substantially improves the activity and stability of enzymes in aqueous solution. Most “long” linkers (e.g. polyethylene oxide derivatives) are relatively hydrophilic, improving the solubility of the linker-enzyme conjugate in polar environments, but this provides little benefit in non-polar environments such as organic solvents. We present a novel method for the covalent immobilization of enzymes on solid surfaces using a long, hydrophobic polytryptophan tether. Candida antarctica lipase B (CALB) was covalently immobilized on non-porous, functionalized 1-μm silica microspheres, with and without an intervening hydrophobic poly-DL-tryptophan tether (n ≈ 78). The polytryptophan-tethered enzyme exhibited 35 times greater esterification of n-propanol with lauric acid in the organic phase and five times the hydrolytic activity against pnitrophenol palmitate, compared to the activity of the same enzyme immobilized without tethers. In addition, the hydrophobic tethers caused the silica microspheres to disperse more readily in the organic phase, while the surface-immobilized control treatment was less lipophilic and quickly settled out of the organic phase when the suspensions were not vigorously mixed.

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Development of a thiol‐ene based screening platform for enzyme immobilization demonstrated using horseradish peroxidase

Hoffmann

Pinelo

Woodley

et al. 2017

Biotechnology Progress

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Efficient immobilization of enzymes on support surfaces requires an exact match between the surface chemistry and the specific enzyme. A successful match would normally be identified through time consuming screening of conventional resins in multiple experiments testing individual immobilization strategies. In this study we present a versatile strategy that largely expands the number of possible surface functionalities for enzyme immobilization in a single, generic platform. The combination of many individual surface chemistries and thus immobilization methods in one modular system permits faster and more efficient screening, which we believe will result in a higher chance of discovery of optimal surface/enzyme interactions. The proposed system consists of a thiol-functional microplate prepared through fast photochemical curing of an off-stoichiometric thiol-ene (OSTE) mixture. Surface functionalization by thiol-ene chemistry (TEC) resulted in the formation of a functional monolayer in each well, whereas, polymer surface grafts were introduced through surface chain transfer free radical polymerization (SCT-FRP). Enzyme immobilization on the modified surfaces was evaluated by using a rhodamine labeled horseradish peroxidase (Rho-HRP) as a model enzyme, and the amount of immobilized enzyme was qualitatively assessed by fluorescence intensity (FI) measurements. Subsequently, Rho-HRP activity was measured directly on the surface. The broad range of utilized surface chemistries permits direct correlation of enzymatic activity to the surface functionality and improves the determination of promising enzyme-surface candidates. The results underline the high potential of this system as a screening platform for synergistic immobilization of enzymes onto thiol-ene polymer surfaces. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:1267-1277, 2017.

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Covalent Enzyme Immobilization

Cited by 8 publications

References 81 publications

Poly (acrylonitrile-co-methyl methacrylate) nanoparticles: I. Preparation and characterization

Poly (acrylonitrile-co-methyl methacrylate) nanoparticles: I. Preparation and characterization

Activation of immobilized lipase in non‐aqueous systems by hydrophobic poly‐DL‐tryptophan tethers

Development of a thiol‐ene based screening platform for enzyme immobilization demonstrated using horseradish peroxidase

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