Immobilization of β-Glucosidase on carbon nanotubes

Gómez, J.M.; Romero, M.D.; Fernández, T. Meixús

doi:10.1007/s10562-005-4904-4

Cited by 60 publications

(27 citation statements)

References 21 publications

(18 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Both approaches have their advantages and shortcomings [3][4][5][6]. The advantage of adsorption is simplicity, as usually no cross-linking reagents or activation steps are required.…”

mentioning

confidence: 99%

Immobilization of Fungal β-Glucosidase on Silica Gel and Kaolin Carriers

Karagulyan¹,

Gasparyan²,

Decker

2007

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Beta-glucosidase is a key enzyme in the hydrolysis of cellulose for producing feedstock glucose for various industrial processes. Reuse of enzyme through immobilization can significantly improve the economic characteristics of the process. Immobilization of the fungal beta-glucosidase by covalent binding and physical adsorption on silica gel and kaolin was conducted for consequent application of these procedures in large-scale industrial processes. Different immobilization parameters (incubation time, ionic strength, pH, enzyme/support ratio, glutaric aldehyde concentration, etc.) were evaluated for their effect on the thermal stability of the immobilized enzyme. It was shown that the immobilized enzyme activity is stable at 50 degrees C over 8 days. It has also been shown that in the case of immobilization on kaolin, approximately 95% of the initial enzyme was immobilized onto support, and loss of activity was not observed. However, covalent binding of the enzyme to silica gel brings significant loss of enzyme activity, and only 35% of activity was preserved. In the case of physical adsorption on kaolin, gradual desorption of enzyme takes place. To prevent this process, we have carried out chemical modification of the protein. As a result, after repeated washings, enzyme desorption from kaolin has been reduced from 75 to 20-25% loss.

show abstract

“…Both approaches have their advantages and shortcomings [3][4][5][6]. The advantage of adsorption is simplicity, as usually no cross-linking reagents or activation steps are required.…”

mentioning

confidence: 99%

Immobilization of Fungal β-Glucosidase on Silica Gel and Kaolin Carriers

Karagulyan¹,

Gasparyan²,

Decker

2007

Appl Biochem Biotechnol

View full text Add to dashboard Cite

show abstract

“…It is worth noting that even physical adsorption of enzymes onto carbon surfaces may induce secondary structural perturbations as a result of protein interaction with the carbon surface, 495 and that substantial perturbation can induce either nearly complete loss 505 or significant increases 506,507 in catalytic activity. Structural and biochemical characterization have revealed that the curvature of the carbon nanomaterial affects the immobilization yield, the catalytic behavior and the secondary structure of enzymes.…”

Section: Cnts For Enzyme Immobilizationmentioning

confidence: 99%

“…507 Recent works have also emphasized biocatalysis with carbon nanomaterials for enzyme-based biofuel cells, 525 and encouraging results have been reported on the use of enzyme-nanocarbon composites for electrocatalytic H 2 oxidation, 526,527 oxygen reduction 528 , glucose oxidation, 529,530 or ethanol oxidation. 531 In order to produce effective and recyclable catalysts for enantioselective trans-esterification in industrial applications, alkaline lipase from Pseudomonas fluorescens was non-covalently immobilized on pristine and oxidized MWCNTs.…”

Section: Cnts For Enzyme Immobilizationmentioning

confidence: 99%

Heterogeneous Catalysis on Nanostructured Carbon Material Supported Catalysts

2015

Nanostructured Carbon Materials for Catalysis

View full text Add to dashboard Cite

For almost twenty years there has been an increasing interest in the use of nanostructured carbon materials as catalyst supports. 1-16 Following the nanotechnology wave, a wide variety of carbon nanomaterials has been investigated as catalyst supports, including fullerenes, CNTs, CNFs, carbon onions, nanodiamonds, FLG or GO. CNTs and CNFs, which constitute a new family of support offering a good compromise between the advantages of AC and high surface area graphite have been particularly studied. The main advantages offered by CNT or CNF supports are: 17 (i) the high purity of the material can avoid self-poisoning; (ii) the mesoporous nature of these supports can be of interest for liquid-phase reactions, thus limiting the mass transfer; (iii) the high thermal conductivity that limits hot-spots that can damage the catalyst; (iv) their well-defined and tunable structure; (v) their rich surface chemistry that offers numerous perspectives for adsorption and dispersion of the active phase; and (vi) the specific metal support interactions, due to high electrical conductivity of the support and to the tunable orientation of the graphene layers, that exist and that can directly affect catalytic activity and selectivity. The possibility to perform catalysis in a confined space is also of great interest. 6,18 From a theoretical viewpoint, graphene provides the ultimate two-dimensional model of a catalytic support. The reason is related to its high theoretical surface area (ca. 2630 m 2 g −1 ), high conductivity, unique graphitized basal plane structure and chemical tolerance. FLG,

show abstract

“…8 They are increasingly attracting attention as the nano-scale materials for potential biological applications. [9][10][11][12][13][14][15][16] A useful type of applications is illustrated by their use as nano-scale supporters for immobilizing enzyme leading to biosensors and nanobiocatalysts. Carbon nanotubes, particularly single walled carbon nanotubes, have a large surface area, thus enabling the high loading of enzymes and lowering diffusional resistance.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Lipase on Single Walled Carbon Nanotubes in Ionic Liquid

Lee¹,

Lee²,

Kim³

et al. 2010

Bulletin of the Korean Chemical Society

View full text Add to dashboard Cite

A lipase from Pseudomonas cepacia was immobilized onto single walled carbon nanotubes (SWNTs) in two different ways in each of two solvent systems (buffer and ionic liquid). The most efficient immobilization was achieved in ionic liquid (1-butyl-3-methylimidazolium tetrafluoroborate, BMIM-BF4). In this procedure, carbon nanotubes were first functionalized noncovalently with 1-pyrenebutyric acid N-hydroxysuccinimide ester and then subject to the coupling reaction with the lipase in ionic liquid. The resulting immobilized enzyme displayed the highest activity in the transesterification of 1-phenylethyl alcohol in the presence of vinyl acetate in toluene.

show abstract

Immobilization of β-Glucosidase on carbon nanotubes

Cited by 60 publications

References 21 publications

Immobilization of Fungal β-Glucosidase on Silica Gel and Kaolin Carriers

Immobilization of Fungal β-Glucosidase on Silica Gel and Kaolin Carriers

Heterogeneous Catalysis on Nanostructured Carbon Material Supported Catalysts

Immobilization of Lipase on Single Walled Carbon Nanotubes in Ionic Liquid

Contact Info

Product

Resources

About