Catalase encapsulated in mesoporous silica and its performance

Itoh, Tetsuji; Ishii, Ryo; Matsuura, Shun-ichi; Hamakawa, Satoshi; Hanaoka, Toshiaki; Tsunoda, Tetsuto; Mizuguchi, Junko; Mizukami, Fujio

doi:10.1016/j.bej.2008.11.015

Cited by 36 publications

(34 citation statements)

References 22 publications

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“…There are also techniques that, in a direct way, measure enzyme molecules localized inside the material. These techniques are fluorescence microscopy [59,63,64] and transmission electron microscopy in combination with immunogold staining (TEM-IGS) [65] that will be described in section 3.3. N 2 sorption is a standard method for characterizing the pore size, specific surface area, pore volume and geometry of porous materials (See section 2) [25].…”

Section: Indirect Techniques That Demonstrate That the Enzymes Are Inmentioning

confidence: 99%

“…By labeling a protein with a fluorescent dye prior to immobilization the protein can be imaged directly with fluorescence microscopy [59,63,64]. When Cy5-labeled BSA was immobilized in large mesoporous silica particles (150-425 µm in diameter) with varying pore size (2.2-45 nm) it was observed that the proteins entered further into the pores with increasing pore size, although a majority of the BSA molecules were adsorbed at the outer surface and at the pore entrances of the particles [63].…”

Section: Direct Visualization Of Immobilized Enzymesmentioning

confidence: 99%

“…Techniques commonly used for this purpose are N 2 adsorption [11] [56][57][58][59], X-ray diffraction (XRD) [11], Fourier transform infrared spectroscopy (FTIR) [60,61] and thermogravimetric analysis (TGA) [52,62]. These are here referred to as indirect techniques.…”

Section: Indirect Techniques That Demonstrate That the Enzymes Are Inmentioning

confidence: 99%

“…N 2 sorption is a standard method for characterizing the pore size, specific surface area, pore volume and geometry of porous materials (See section 2) [25]. It is also common to use the technique to evaluate pore occupation by measuring N 2 adsorption before and after protein immobilization [11] [ [56][57][58][59]. For instance, a lower amount of N 2 adsorption after trypsin immobilization to SBA-15 compared to the adsorption to pure support material was translated into reduced available pore volume, surface area and pore size [58].…”

Section: Indirect Techniques That Demonstrate That the Enzymes Are Inmentioning

confidence: 99%

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Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Carlsson

Gustafsson

Thörn

et al. 2014

Advances in Colloid and Interface Science

211

167

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Section: Indirect Techniques That Demonstrate That the Enzymes Are Inmentioning

confidence: 99%

Section: Direct Visualization Of Immobilized Enzymesmentioning

confidence: 99%

Section: Indirect Techniques That Demonstrate That the Enzymes Are Inmentioning

confidence: 99%

Section: Indirect Techniques That Demonstrate That the Enzymes Are Inmentioning

confidence: 99%

See 2 more Smart Citations

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Carlsson

Gustafsson

Thörn

et al. 2014

Advances in Colloid and Interface Science

211

167

View full text Add to dashboard Cite

“…Adsorption, encapsulation, entrapment and covalent binding (Kondo et al, 1993;Alptekin et al, 2008Alptekin et al, , 2009Alptekin et al, and 2010Itoh et al, 2009) have been used to immobilize CAT. However, Wilson et al (2004) reported that these methods are difficult to stabilize the CAT quaternary structure.…”

Section: Introductionmentioning

confidence: 99%

Cross-Linked Enzyme Aggregates of Catalase From Bovine Liver

Mafra¹,

Kopp²,

Ramos³

et al. 2015

Anais Do XX Congresso Brasileiro De Engenharia Química

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-Stabilization of multimeric enzymes is one of the major challenges in biocatalysis, because dissociation of subunits can inactivate the enzyme. Catalase (CAT; EC 1.11.16) is a homotetramer containing Fe-protoporphyrin IX in its active site. CAT breaks down hydrogen peroxide into water and molecular oxygen. In this study, crosslinked enzyme aggregates of bovine liver CAT (CAT-CLEAs) were prepared. The effects of precipitation and cross-linking on enzyme activity were studied. Thermal stability of free and immobilized enzyme were also evaluated at 40 ᵒC and pH 7 (200 h). CAT-CLEAs were successfully prepared using ammonium sulfate and glutaraldehyde (50 mM) as the precipitant and cross-linking agent, respectively. The best recovered activity obtained was 62 %. The derivative retained high activity along the stability test. The kinetic parameters values v max and K m were estimated as 11,350 U/mg and 66.7±10 mM for the free CAT and 2,000 U/mg and 392±22 mM for the CAT-CLEAs, respectively.

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A kinetic analysis of catalytic production of oxygen in catalase‐containing liposome dispersions for controlled transfer of oxygen in a bioreactor

Yoshimoto¹,

Higa

2013

J of Chemical Tech & Biotech

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BACKGROUND: Biochemical oxidation reactions require oxygen to be supplied by dispersed bubbles. Drawbacks of the gas-liquid system are enzyme denaturation and low oxygen utilization efficiency. Therefore, oxygen production through the decomposition of H 2 O 2 is useful for controlled oxygen transfer in bioreactors. RESULTS:Catalase-containing liposomes (CALs) were prepared in 50 mmol L -1 Tris/0.1 mol L -1 NaCl buffer (pH 7.4) and the kinetic model was developed for the oxygen production by CAL-catalyzed decomposition of 1.0 mmol L -1 H 2 O 2 . Applying the model to the observed time course of oxygen produced gave overall resistance in the reaction based on the pseudo-steadystate assumption inside liposomes for H 2 O 2 and oxygen. The reaction resistance was estimated with the liposomal catalase concentration e t,in and the kinetic parameters of free enzyme reaction. At e t,in = 0.59 μmol L -1 , the CAL reaction proceeded under reaction control, while at e t,in = 5.05 μmol L -1 , the H 2 O 2 transfer resistance was involved. For the latter case, the permeability coefficient P P of H 2 O 2 through the liposome membrane was determined as 1.06 × 10 -6 m s -1 at 25 • C. The model predicted the H 2 O 2 concentration inside liposomes with different e t,in values. Furthermore, the oxygen concentration in the CAL dispersions was reasonably simulated. The oxygen production rate could be altered based on temperature (10-55 • C) and the fractional volume of CALs. CONCLUSION: The CAL-catalyzed oxygen production was controlled based on the e t,in and P P values, which determine the relative importance of the reaction and H 2 O 2 transfer resistances. The CAL would be applied to oxidation reactions instead of gas-liquid systems.

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Catalase encapsulated in mesoporous silica and its performance

Cited by 36 publications

References 22 publications

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Enzymes immobilized in mesoporous silica: A physical–chemical perspective

Cross-Linked Enzyme Aggregates of Catalase From Bovine Liver

A kinetic analysis of catalytic production of oxygen in catalase‐containing liposome dispersions for controlled transfer of oxygen in a bioreactor

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