Immobilized enzymes in ordered mesoporous silica materials and improvement of their stability and catalytic activity in an organic solvent

Takahashi, Hitomi; Li, Bo; Sasaki, Taro; Miyazaki, Chikara; Kajino, Toshitaka; Inagaki, Shinji

doi:10.1016/s1387-1811(01)00257-8

Cited by 274 publications

(189 citation statements)

References 23 publications

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“…When FDH molecules were embedded in the carbon mesopores with pore sizes comparable to that of the enzyme, an enhanced contact area between FDH and the carbon surface led to a strong adsorption of FDH on the carbon surface as well as to enzyme stabilization by preventing the denaturation, aggregation and collision of enzyme molecules. Although the stability and activity of enzymes have been shown to be improved by loading them on mesoporous nonelectroconductive materials such as mesoporous silica and polymer beads with a suitable pore size for the enzymes, [24][25][26] this is the first report, to the best of our knowledge, demonstrating that mesoporous carbon materials offer a high specific surface area as well as effective space for encaging enzyme molecules, resulting in a stable and enhanced catalytic current.…”

Section: ¹2mentioning

confidence: 97%

Effect of Pore Size of MgO-templated Carbon on the Direct Electrochemistry of <small>D</small>-fructose Dehydrogenase

2015

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MgO-templated porous carbon (MgOC) was developed for D-fructose dehydrogenase (FDH) electrodes. MgOCs with an average pore diameter ranging from 10 to 100 nm were used in this study. FDH adsorbed on a MgOC electrode exhibited significant catalytic currents for D-fructose-oxidation without a redox mediator. When the pore size of MgOC was much larger than the size of FDH, a sufficient amount of FDH was adsorbed in the mesopore on and even inside the MgOC structure. In contrast, when the pore size of MgOC was comparable to the size of FDH, the catalytic current depended only on the amount of enzyme adsorbed in mesopores formed at the surface of the carbon particles; however, an enhanced thermal stability of FDH was observed. Thus, FDH was stabilized through encaging in carbon mesopores with a size comparable to that of the enzyme.

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Section: ¹2mentioning

confidence: 97%

Effect of Pore Size of MgO-templated Carbon on the Direct Electrochemistry of <small>D</small>-fructose Dehydrogenase

2015

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“…No covalent immobilization is needed provided the pores have suitable diameter; the soluble catalyst resides in the pores and meets the substrate 45 at the pore openings. Particles loaded with an enzyme or a homogeneous catalyst in the waterfilled pores are either dispersed in an aqueous [1][2][3][4] or a non-aqueous [6,7] solution in which the reactants are dissolved. The reverse has also been described: particles with hydrophobized pores housing a hydrophobic homogeneous catalyst dissolved in an apolar medium and with water as the surrounding phase [5].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica—The effect of varied particle size and morphology

Gustafsson

Johansson

Barrabino

et al. 2012

Colloids and Surfaces B: Biointerfaces

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Immobilization of enzymes usually improves the recyclability and stability and can sometimes also improve the activity compared to enzymes free in solution. Mesoporous silica is a widely studied material as host for immobilized enzymes because of its large internal surface area and tunable pores. It has previously been shown that the pore size is critical both for the loading capacity and for the enzymatic activity; however, less focus has been given to 20 the influence of the particle size. In this work the effect of particle size and particle morphology on the immobilization of lipase from Mucor miehei and Rhizopus oryzae have been investigated. Three kinds of mesoporous silica, all with 9 nm pores but with varying particle size (1000 nm, 300 nm and 40 nm) have been synthesized and were used as host for the lipases. The two lipases, which have the same molecular size but widely different 25 isoelectric points, were immobilized into the silica particles at varied pH values within the interval 5 to 8. The 300 nm particles were proven to be the most suitable carrier with respect to specific activity for both enzymes. The lipase from Mucor miehei was more than four times as active when immobilized at pH 8 compared to free in solution whereas the difference was less pronounced for the Rhizopus oryzae lipase. 30

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“…23 In this work, we studied the THz-TD spectra of aromatic carboxylic acids, namely o-phthalic acid, benzoic acid, and salicylic acid, which form either intra-or intermolecular hydrogen bond(s) in different ways, and compared the spectra of molecules incorporated in the nano-sized pores of SBA-16 and bulk crystal samples. We also report the differences in the temperature-dependent peak shifts caused by the different nature of the THz absorption.…”

Section: Introductionmentioning

confidence: 99%

Terahertz Time-domain Spectra of Aromatic Carboxylic Acids Incorporated in Nano-sized Pores of Mesoporous Silicate

Ueno

Ajito

2007

ANAL. SCI.

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Immobilized enzymes in ordered mesoporous silica materials and improvement of their stability and catalytic activity in an organic solvent

Cited by 274 publications

References 23 publications

Effect of Pore Size of MgO-templated Carbon on the Direct Electrochemistry of <small>D</small>-fructose Dehydrogenase

Effect of Pore Size of MgO-templated Carbon on the Direct Electrochemistry of <small>D</small>-fructose Dehydrogenase

Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica—The effect of varied particle size and morphology

Terahertz Time-domain Spectra of Aromatic Carboxylic Acids Incorporated in Nano-sized Pores of Mesoporous Silicate

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