Mesoporous materials as host for an entrapped enzyme

Reis, Pedro; Witula, Tomasz; Holmberg, Krister

doi:10.1016/j.micromeso.2007.06.025

Cited by 50 publications

(32 citation statements)

References 21 publications

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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%

“…The systems are robust and the work-up procedure is extremely facile; the catalyst-loaded particles are simply removed from the reaction mixture by filtration or centrifugation. It has been shown both for an enzyme [6] and for a synthetic homogeneous catalyst [5] that the loaded particles can be reused several cycles. 55…”

Section: Introductionmentioning

confidence: 99%

“…Most mesoporous materials used as host for soluble catalysts are silicates but other mesoporous oxides, such as alumina and titania have also been employed for the purpose [6]. The materials are made by a templating procedure, using an organic template that is subsequently removed by solvent extraction or by 60 calcination or by a combination of these.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…Coating lipases with surfactant 7 and ionic liquid 8 has been developed to increase the solubility of lipases. In addition, immobilization of lipases onto solid supports 9 (lipase trapped in polymers 10,11 or solÀgel materials, 12,13 and lipase immobilized on modified nanoparticles 14À16 or mesoporous materials 17 ) is also used to improve the dispersion state of lipases and enhance the enzymatic activity. Currently, a popular trend is the use of mesoporous silicates as supports for lipase immobilization.…”

Section: Introductionmentioning

confidence: 99%

Hydrophobic Surface Induced Activation of Pseudomonas cepacia Lipase Immobilized into Mesoporous Silica

et al. 2011

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“…19 The reaction proceeded well with all three oxides but alumina gave considerably higher conversion than the other two, see Figure 9. Hydrophobized silica gave an even higher degree of esterification.…”

Section: Biocatalysis With a Lipase Entrapped In The Pores Of Mesopormentioning

confidence: 87%

Use of ordered mesoporous materials as tools for organic and bioorganic synthesis

Handa¹,

Witula²,

Reis³

et al. 2008

Arkivoc

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Ordered mesoporous materials are materials with well defined pore sizes in the range of 2 to 50 nm. This paper shows that suspensions of particles of mesoporous materials can be useful tools for organic and bioorganic synthesis. They can be used to overcome reactant incompatibility, as is demonstrated for a reaction between 4-tert-butylbenzyl bromide and KI. The pores are impregnated with an aqueous solution of KI and the lipophilic reactant is present in the continuous apolar phase. The reaction occurs at the pore openings. The pores of the mesoporous material can also be used as host for a homogeneous catalyst. The catalyst-loaded particles are kept as a suspension in a medium that contains the reactants. This principle is demonstrated for a Heck-type reaction with a watersoluble rhodium catalyst inserted into the pores of mesoporous silica. It is also shown to work well for a 1,4-conjugate addition between two water-soluble reactants, 4-carboxyphenylboronic acid and methyl acrylate, in which case a toluene-soluble rhodium catalyst was entrapped in the pores of hydrophobized mesoporous silica. The same principle was also used for biocatalysis. Lipase was inserted into either hydrophilic or hydrophobic pores and used for both ester synthesis and ester hydrolysis. Finally, palladium nanoparticles were deposited inside the pores of mesoporous carbon and used as catalyst for a Sonogashira reaction.

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Mesoporous materials as host for an entrapped enzyme

Cited by 50 publications

References 21 publications

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

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

Hydrophobic Surface Induced Activation of Pseudomonas cepacia Lipase Immobilized into Mesoporous Silica

Use of ordered mesoporous materials as tools for organic and bioorganic synthesis

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