Mesoporous molecular sieve immobilized enzymes

Gimon-Kinsel, Mary E.; Jimenez, V.L.; Washmon, L.; Balkus, Kenneth J.

doi:10.1016/s0167-2991(98)81014-8

Cited by 62 publications

(36 citation statements)

References 15 publications

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“…These data also showed a clear dependence of the adsorbed amount on pore size. 76 During the first few years, immobilization of enzymes in OMSs did not stimulate many researchers to enter this new field. However, the fast developments in the synthesis of larger pore OMSs such as the use of organics (e.g.…”

Section: Immobilization Of Enzymesmentioning

confidence: 99%

Progress in enzyme immobilization in ordered mesoporous materials and related applications

2013

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A short time after the discovery of ordered mesoporous materials, which possess unique features such as high specific surface area and pore volume, highly uniform pore distribution and tunable pore size, these materials have been prospected as promising carriers for enzyme immobilization. The immobilization of enzymes in ordered mesoporous materials has been studied for almost two decades. With the development of tailored ordered mesoporous materials and advances in enzyme technology, this field attracted increasing interest due to its quickly expanded functions and applications. This review focuses on the relation between the progress in ordered mesoporous materials and its corresponding contribution to enzyme immobilization as well as the applications of these materials in biocatalysis. The potential trends in the future development of this field are also pointed out.

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Section: Immobilization Of Enzymesmentioning

confidence: 99%

Progress in enzyme immobilization in ordered mesoporous materials and related applications

2013

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“…[73][74][75][76][77] However, constant mesopore volume is evidence for adsorption only on the external surface of the mesoporous material. [78][79][80] XRD analysis before and after adsorption of a protein can indicate retention of the mesoporous structure and also entry of the protein into the mesopores by a reduction in the intensity of the reflection peaks. [74,75,78,[81][82][83] …”

Section: Relative Size Of the Mesopores And The Proteinmentioning

confidence: 99%

Proteins in Mesoporous Silicates

2008

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Mesoporous silicates (MPS) have an ordered pore structure with dimensions comparable to many biological molecules. They have been extensively explored as supports for proteins and enzymes in biocatalytic applications. Since their initial discovery, novel syntheses methods have led to precise control over pore size and structure, particle size, chemical composition, and stability, thus allowing the adsorption of a wide variety of biological macromolecules, such as heme proteins, lipases, antibody fragments, and proteases, into their structures. This Review discusses the application of ordered, large-pore, functionalized mesoporous silicates to immobilize proteins for biocatalysis.

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“…At the modified electrode prepared with ODA-HMS, the couple of redox peaks occurring at more negative potentials showed larger currents than that at the modified electrode prepared with DDA-HMS, and the couple of redox peaks occurring at more positive potentials showed smaller currents than that at the modified electrode prepared with DDA-HMS. Considering the fact that enzyme can be fixed in the pores of mesoporous materials by simply immersing the mesoporous materials in the enzyme solution [36,37] and the larger pore diameter of ODA-HMS (4.04 nm) than that of DDA-HMS (3.35 nm), more HRP molecules could intercalate into the mesopores of ODA-HMS. The changes in peak currents resulted from the changes of the amounts of HRP molecules intercalated in the mesopores and adsorbed on the external surface of HMS.…”

Section: Intercalation Of Hrp In the Mesopores Of Hmsmentioning

confidence: 99%

Mesoporous Materials Promoting Direct Electrochemistry and Electrocatalysis of Horseradish Peroxidase

Dai

Chen

2005

Electroanalysis

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The direct electron transfer and electrocatalysis of horseradish peroxidase (HRP) immobilized on hexagonal mesoporous silicas (HMS) matrix was studied. The interaction between HRP and HMS was examined by using Fourier transform infrared spectroscopy, nitrogen adsorption isotherms and electrochemical methods. The immobilized HRP at a modified glassy carbon electrode showed a good direct electrochemical behavior, which depended on the specific properties of the HMS. Two couples of redox peaks corresponding to Fe(III) to Fe(II) conversion of the HRP intercalated in the mesopores and adsorbed on the external surface of the HMS were observed with the formal potentials of À 0.315 and À 0.161 V in 0.1 M pH 7.0 PBS, respectively. The amount of HRP intercalated in the mesopores of HMS proved to be related to the pore size. The HRP intercalated in the mesopores showed a surface controlled electrode process with a single proton transfer. The immobilized HRP displayed an excellent electrocatalytic response to the reduction of hydrogen peroxide (H 2 O 2 ) without the aid of an electron mediator. The HMS provided a novel matrix for protein immobilization and direct electron transfer study of the immobilized protein.

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Mesoporous molecular sieve immobilized enzymes

Cited by 62 publications

References 15 publications

Progress in enzyme immobilization in ordered mesoporous materials and related applications

Progress in enzyme immobilization in ordered mesoporous materials and related applications

Proteins in Mesoporous Silicates

Mesoporous Materials Promoting Direct Electrochemistry and Electrocatalysis of Horseradish Peroxidase

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