Highly efficient immobilization of glycosylated enzymes into polyurethane foams

Bakker, Martin G.; Velde, Fred van de; Rantwijk, Fred van; Sheldon, Roger A.

doi:10.1002/1097-0290(20001105)70:3<342::aid-bit11>3.0.co;2-a

Cited by 35 publications

(14 citation statements)

References 27 publications

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“…The advantages of this assay are that the process is faster and higher activity retention could be obtained. [33][34][35][36]40 Although PUs are widely used supports for immobilization of enzymes and cells, 33,[35][36][37]40 to the best of the author's knowledge, the CA has not been immobilized within PU foam. In the present work, the CA was immobilized within PU foam covalently by cross-linking for the biomimetic CO 2 sequestration purposes.…”

Section: Introductionmentioning

confidence: 99%

Biomimetic CO₂Sequestration: 1. Immobilization of Carbonic Anhydrase within Polyurethane Foam

Ozdemir¹

2009

Energy Fuels

103

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Bovine carbonic anhydrase (CA) was immobilized within polyurethane (PU) foam for biomimetic CO 2 sequestration. The catalytic activities for the free and immobilized CA were estimated using paranitrophenyl acetate (p-NPA) as the substrate. Because the p-NPA has limited solubility in the aqueous phase, the activities were estimated in Tris buffer containing 10% acetonitrile. A Lineweaver-Burk relationship was employed to estimate the Michaelis-Menten kinetic parameters for the free and immobilized CA. The k cat , K m , and k cat /K m values for the free CA were found to be 2.02 s , respectively. The K m value for the immobilized CA was estimated to be 9.6 mM at the same conditions. The immobilized CA was stable and did not lose any activity over seven consecutive washings and activity tests. While the free CA lost its activity in 45 days stored at 4°C in refrigerator, the immobilized CA maintained 100% of its activity over a 45 day period stored in Tris buffer at ambient conditions. It was concluded that the immobilized CA as a very stable biocatalyst could be employed in biomimetic CO 2 sequestration.

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Section: Introductionmentioning

confidence: 99%

Biomimetic CO₂Sequestration: 1. Immobilization of Carbonic Anhydrase within Polyurethane Foam

Ozdemir¹

2009

Energy Fuels

103

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“…In the case of powdered polyurethane, only covalent binding between amino groups of the β-galactosidase and isocyanate groups of polyurethane may cause immobilization. With polyurethane foam, entrapment in the micropores assists the immobilization of β-galactosidase [29]. In both cases the efficiency of immobilization increased in parallel with the ratio of diisocyanate/diol components ( Table 1, No.…”

Section: Atmentioning

confidence: 99%

“…2 Effect of pH on the activity of β-galactosidase immobilized on chitosan (1) and native β-galactosidase (2). zymes [3,29]. We used foamable and powdery polyurethane for immobilization of β-galactosidase.…”

Section: Atmentioning

confidence: 99%

β-Galactosidase from Penicillium canescens. Properties and immobilization

et al. 2005

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β-galactosidase from Penicillium canescens was immobilized on chitosan, sepharose-4B, foamable polyurethane and some other carriers. The highest yield of immobilization (up to 98 %) was obtained by using chitosan as a carrier. The optimum pH and temperature were not significantly altered by immobilization. High stability of immobilized β-galactosidase during storage was demonstrated. Efficient lactose saccharification (over 90 %) in whey was achieved by using immobilized β-galactosidase.

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“…On the other hand, there are a large number of reports regarding CPO immobilization [for representative examples, see [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25], showing a broad range of enzyme load and retained activity. Reported immobilization techniques range from the use of typical methods such as physical adsorption onto mesoporous materials, talc, and others to the combination of several methods such as CLEA's entrapment in mesoporous materials.…”

Section: Introductionmentioning

confidence: 99%

Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase

Salcedo¹,

Torres

Haces

et al. 2015

Biocatalysis

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Chloroperoxidase fromCaldariomyces fumago was immobilized in Eupergit ® C, a commercial mesoporous acrylic-based material. Due to low stability of the enzyme under neutral and basic pH, the usual covalent immobilization procedures cannot be applied to this enzyme. Several strategies were followed in order to achieve a stable interaction between the protein and the support. The support was efficiently functionalized with different reactive groups such as aromatic and aliphatic amines, glutaraldehyde, diazonium ions, and maleimide moieties; solvent-exposed amino acid residues in chloroperoxidase were identified or created through chemical modification, so that they were reactive under conditions where the enzyme is stable. Enzyme load and retained activity were monitored, obtaining biocatalysts with specific activity ranging from 200 to 25,000 U/g. The highest load and activity was obtained from the immobilization of a chemically-modified CPO preparation bearing a solvent-exposed free thiol group. This biocatalyst efficiently catalyzed the transformation of β-estradiol, an endocrine disruptor.

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Highly efficient immobilization of glycosylated enzymes into polyurethane foams

Cited by 35 publications

References 27 publications

Biomimetic CO₂Sequestration: 1. Immobilization of Carbonic Anhydrase within Polyurethane Foam

Biomimetic CO₂Sequestration: 1. Immobilization of Carbonic Anhydrase within Polyurethane Foam

β-Galactosidase from Penicillium canescens. Properties and immobilization

Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase

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Highly efficient immobilization of glycosylated enzymes into polyurethane foams

Cited by 35 publications

References 27 publications

Biomimetic CO2Sequestration: 1. Immobilization of Carbonic Anhydrase within Polyurethane Foam

Biomimetic CO2Sequestration: 1. Immobilization of Carbonic Anhydrase within Polyurethane Foam

β-Galactosidase from Penicillium canescens. Properties and immobilization

Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase

Contact Info

Product

Resources

About

Biomimetic CO₂Sequestration: 1. Immobilization of Carbonic Anhydrase within Polyurethane Foam

Biomimetic CO₂Sequestration: 1. Immobilization of Carbonic Anhydrase within Polyurethane Foam