Surface-initiated enzymatic vinyl polymerization: synthesis of polymer-grafted silica particles using horseradish peroxidase as catalyst

Fukushima, Haruka; Kohri, Michinari; Kojima, Takashi; Taniguchi, Tadatsugu; Saito, Kyoichi; Nakahira, Takayuki

doi:10.1039/c2py20036h

Cited by 28 publications

(11 citation statements)

References 29 publications

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“…Consequently, through the phosphamide bond a versatile procedure to obtain hybrid organic-inorganic molecules able to produce the covalent attachment to inorganic supports of many different organic molecules, including biomolecules like lipase enzymes, is achieved. Thus, within the same general schemes currently used with silanized SiO 2 [74][75][76][77], these organic molecules can be modified following the experimental methodology of the solid-phase synthesis, to obtain adequate ligands linked to the solid surfaces [48][49][50][51][52][53][54][55].…”

Section: Discussionmentioning

confidence: 99%

Biofuel that Keeps Glycerol as Monoglyceride by 1,3-Selective Ethanolysis with Pig Pancreatic Lipase Covalently Immobilized on AlPO4 Support

et al. 2013

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By using pig pancreatic lipase (EC 3.1.1.3 or PPL) as a biocatalyst, covalently immobilized on amorphous AlPO 4 support, a new second generation biodiesel was obtained in the transesterification reaction of sunflower oil with ethanol. The resulting biofuel is composed of fatty acid ethyl esters and monoglycerides (FAEE/MG) blended in a 2:1 molar ratio. This novel product, which integrates glycerol as monoacylglycerols (MG) into the biofuels composition, has similar physicochemical properties as conventional biodiesel and also avoids the removal step of the by-product by washing of the biodiesel with water. Immobilization of PPL was achieved by covalent attachment of the ε-amino group of the lysine residues of PPL with the aldehyde groups of p-hydroxybenzaldehyde linked on a hybrid organic-inorganic functionalized AlPO 4 surface. With this procedure, the PPL biocatalyst was strongly fixed to the inorganic support surface (94.3%). Nevertheless, the efficiency of the immobilized enzyme was relatively lower compared to that of the free PPL, but it showed a remarkable stability as well as a great capacity of reutilization (25 reuses) without a significant loss of its initial OPEN ACCESSEnergies 2013, 6 3880 catalytic activity. Therefore, this enzymatic method allows the production of a biodiesel which integrates the glycerol, allows a more efficient fabrication method and minimizes the waste production as compared to the conventional alkali-catalyzed process.

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Section: Discussionmentioning

confidence: 99%

Biofuel that Keeps Glycerol as Monoglyceride by 1,3-Selective Ethanolysis with Pig Pancreatic Lipase Covalently Immobilized on AlPO4 Support

et al. 2013

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“…[16][17][18] Examples are the enzymatic synthesis of polyhydroxyalkanoates on surfaces, 19,20 lipase-catalyzed ring-opening polymerizations of ε-caprolactone, 21,22 as well as peroxidase-mediated radical polymerization of aniline [23][24][25][26] and acrylamide. 27,28 Moreover, surface-initiated enzymatic polymerizations of DNA by terminal deoxynucleotidyl transferase have been explored to amplify signals in biosensing. [29][30][31][32][33][34] Recently, we and others have shown that metalloproteins such as hemoglobin (Hb), horseradish peroxidase, and laccase can catalyze ATRP in solution [35][36][37][38][39][40][41][42] and on surfaces.…”

Section: Introductionmentioning

confidence: 99%

Controlling Enzymatic Polymerization from Surfaces with Switchable Bioaffinity

et al. 2017

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The affinity of surfaces toward proteins is found to be a key parameter to govern the synthesis of polymer brushes by surface-initiated biocatalytic atom transfer radical polymerization (SI-bioATRP). While the "ATRPase" hemoglobin (Hb) stimulates only a relatively slow growth of protein repellent brushes, the synthesis of thermoresponsive grafts can be regulated by switching the polymer's attraction toward proteins across its lower critical solution temperature (LCST). Poly(N-isopropylacrylamide) (PNIPAM) brushes are synthesized in discrete steps of thickness at temperatures above LCST, while the biocatalyst layer is refreshed at T< LCST. Multistep surface-initiated biocatalytic ATRP demonstrates a high degree of control, results in high chain end group fidelity and enables the synthesis of multiblock copolymer brushes under fully aqueous conditions. The activity of Hb can be further modulated by tuning the accessibility of the heme pocket within the protein. Hence, the multistep polymerization is accelerated at acid pH, where the enzyme undergoes a transition from its native to a molten globule conformation. The controlled synthesis of polymer brushes by multistep SI-bioATRP highlights how a biocatalytic synthesis of grafted polymer films can be precisely controlled through the modulation of the polymer's interfacial physicochemical properties, in particular of the affinity of the surface toward proteins. This is not only of importance to gain a predictive understanding of surface-confined enzymatic polymerizations, but also represents a new way to translate bioadhesion into a controlled functionalization of materials.

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“…Another interesting grafting approach has been reported with silica surfaces using laccases [59] or HRP [60]. In the latter case, for example, SiO 2 particles were first covered with the initiator (Acac) followed by HRP-initiated grafting of acrylamide onto the SiO 2 particle (Scheme 11.10).…”

Section: Selected Examplesmentioning

confidence: 99%