Enzyme immobilisation using siliceous mesoporous molecular sieves

Yiu, Humphrey H. P.; Wright, Paul A.; Botting, Nigel P.

doi:10.1016/s1387-1811(01)00258-x

Cited by 184 publications

(120 citation statements)

References 8 publications

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“…Several examples of enzyme immobilization onto porous silica have been reported [6][7][8][9][10][11][12]. Co-immobilization of enzymes on various platforms is an emerging field, and involves considerations of various factors: spanning from facile access of substrate to the next enzyme in the cascade, optimization of catalytic activity to allow performance of all components, and the stability of enzyme in the solid support [13].…”

Section: Introductionmentioning

confidence: 99%

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

Hsin¹,

Radu²,

Dezayas³

et al. 2017

J Thermodyn Catal

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The successful demonstration of a tandem enzymatic catalyst which utilizes stellate macroporous silica nanospheres (Stellate MSN) platform as dual-enzyme host is reported herein. Upon simultaneous loading of beta-glucosidase and glucose isomerase inside their porous structure, Stellate MSNs-featuring a hierarchical pore arrangement and large surface area, show capability to perform a cascade reaction that converts cellobiose, a cellulosic hydrolysis product, into glucose and further to fructose. The silica platform provides a modality for substrate channelling which involves the transfer of the cascade intermediate, glucose, to the next enzyme without first diffusing to the bulk. A key aspect to this proof-of-concept is the two-enzyme system working in an optimized pH domain to fit the modus operandi for both enzymes. The concept could be extrapolated to other enzyme tandems, with potential to impact dramatically enzymatic processes which require multi-catalyst, one-pot transformations.

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Section: Introductionmentioning

confidence: 99%

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

Hsin¹,

Radu²,

Dezayas³

et al. 2017

J Thermodyn Catal

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“…Ordered mesoporous materials can be used as host for enzymes [1][2][3], as well as for synthetic homogeneous catalysts [4,5]. 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.…”

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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“…150kDa) in FMS, we prepared UMS with a pore size (diameter) as large as 30 nm, a surface area as great as 533 m 2 /g and an average bead size of 12-15 μm (Supporting information).9 , 10 A controlled hydration and condensation reaction was used to introduce functional groups into UMS.9 ,10 Coverage of 2% (or 20%) HOOC-FMS, HO 3 S-FMS or NH 2 -FMS means 2% (or 20%) of the total available silanol groups (5 × 10 18 silanol groups per square meter9 , 10) of UMS would be silanized with trimethoxysilane with the functional group HOOC, HO 3 S or NH 2 . [1][2][3][4][5][6][7] Figs. 1A shows the TEM image of 30 nm 20% HOOC-FMS.…”

mentioning

confidence: 99%

Local Release of Highly Loaded Antibodies from Functionalized Nanoporous Support for Cancer Immunotherapy

Lei¹,

Liu²,

Chen³

et al. 2011

J. Am. Chem. Soc.

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Recent advances with functionalized nanoporous supports provide an innovative approach for entrapping proteins and for their subsequent controlled release and delivery.1 -7 Functionalized mesoporous silica (FMS) can provide a confined and interactive nanoenvironment that increases protein activity and allow large amounts of protein loading compared to unfunctionalized mesoporous silica (UMS) or normal porous silica.5 -7 First, the proteins can be spontaneously entrapped in FMS with rigid, uniform, open nanopore geometry of tens of nanometers via non-covalent interaction. Then, one can control the release of the entrapped proteins from FMS based on the function groups and pore sizes when the FMS-protein composites are dispersed in a fresh buffer solution in which a new thermodynamic balance can be reached. In this work, we found that antibodies can be spontaneously loaded in FMS with super-high density (0.4-0.8 mg of antibody/mg of FMS) due to their comprehensive noncovalent interaction. We hypothesize that therapeutic antibodies entrapped in FMS can be gradually released locally in vivo under physiological conditions and that this will help develop innovative therapies for many diseases. We performed pilot tests to investigate the anti-tumor activity of a monoclonal antibody (mAb) to CTLA4,8 an immunoregulatory molecule released from FMS at the tumor site. This strategy resulted in much greater and extended inhibition of tumor growth than the antibody given systematically.To ensure large loading of mAb molecules (M.W. 150kDa) in FMS, we prepared UMS with a pore size (diameter) as large as 30 nm, a surface area as great as 533 m 2 /g and an average bead size of 12-15 μm (Supporting information).9 , 10 A controlled hydration and condensation reaction was used to introduce functional groups into UMS.9 ,10 Coverage of 2% (or 20%) HOOC-FMS, HO 3 S-FMS or NH 2 -FMS means 2% (or 20%) of the total available silanol groups (5 × 10 18 silanol groups per square meter9 , 10) of UMS would be silanized with trimethoxysilane with the functional group HOOC, HO 3 S or NH 2 . [1][2][3][4][5][6][7] Figs. 1A shows the TEM image of 30 nm 20% HOOC-FMS. There is no significant difference between the TEM images of UMS and their corresponding FMS. 6 Unlike 3-nm and 10-nm mesoporous silica, the 30-nm mesoporous silica has a large degree of disordering, 11 but it still reveals more or less uniform cage-like porous structure. 12 FMS was incubated in the antibody solution, where the antibody would be spontaneously entrapped in FMS. We defined the protein amount (mg) of an antibody entrapped with 1 mg * To whom correspondence should be addressed. chenghong.lei@pnl.gov; hellsk@u.washington.edu; jun.liu@pnl.gov.. 3 Current address: Karolinska Institutet, Department of Oncology-Pathology, SE171-76 Stockholm, Sweden. † These authors contribute equally to this work. Supporting Information Available:Experimental section and additional experimental data are available free of charge via the Internet at http://pubs.acs.org. of FMS as the protein-load...

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Enzyme immobilisation using siliceous mesoporous molecular sieves

Cited by 184 publications

References 8 publications

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

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

Local Release of Highly Loaded Antibodies from Functionalized Nanoporous Support for Cancer Immunotherapy

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