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Development of novel mesoporous sili...

Katiyar, Amit.

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Development of novel mesoporous silicates for bioseparations and biocatalysis.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Development of novel mesoporous silicates for bioseparations and biocatalysis./
作者:	Katiyar, Amit.
面頁冊數:	260 p.
附註:	Adviser: Neville G. Pinto.
Contained By:	Dissertation Abstracts International69-02B.
標題:	Chemistry, Pharmaceutical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3302692
ISBN:	9780549484561

Development of novel mesoporous silicates for bioseparations and biocatalysis.
Katiyar, Amit.

Development of novel mesoporous silicates for bioseparations and biocatalysis. - 260 p.

Adviser: Neville G. Pinto.

Thesis (Ph.D.)--University of Cincinnati, 2008.

The recent growth of the biopharmaceutical industry is due to the discovery of monoclonal antibodies and recombinant DNA technologies. Large-scale production of therapeutic proteins and monoclonal antibodies requires efficient technologies to separate products from complex synthesis mixtures. Chromatography is widely used for this purpose at both the analytical and process scales. Research in the last three decades has provided an improved understanding of the thermodynamic and mass transfer effects underlying the chromatographic behavior of biomolecules, leading to improvements in chromatographic equipment, separation media, and operating procedures.

ISBN: 9780549484561Subjects--Topical Terms:

550957
Chemistry, Pharmaceutical.

Development of novel mesoporous silicates for bioseparations and biocatalysis.
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245 1 0 $a Development of novel mesoporous silicates for bioseparations and biocatalysis.
300 $a 260 p.
500 $a Adviser: Neville G. Pinto.
500 $a Source: Dissertation Abstracts International, Volume: 69-02, Section: B, page: 1022.
502 $a Thesis (Ph.D.)--University of Cincinnati, 2008.
520 $a The recent growth of the biopharmaceutical industry is due to the discovery of monoclonal antibodies and recombinant DNA technologies. Large-scale production of therapeutic proteins and monoclonal antibodies requires efficient technologies to separate products from complex synthesis mixtures. Chromatography is widely used for this purpose at both the analytical and process scales. Research in the last three decades has provided an improved understanding of the thermodynamic and mass transfer effects underlying the chromatographic behavior of biomolecules, leading to improvements in chromatographic equipment, separation media, and operating procedures.
520 $a This dissertation reports on the development of ordered mesoporous silica-based adsorbents for chromatographic protein separations. The synthesis of mesoporous materials with different structural properties is reported here. Protein adsorption and enzymatic catalysis studies were conducted to evaluate the chromatographic performance of these materials. Initial studies focused on small pore materials (MCM-41), which had high protein adsorption capacities. These high protein loadings were attributed to high external surface area (&sim;600 m 2/g), meaning that MCM-41 materials are of limited use for size-selective chromatographic protein separation. Synthesis strategies were developed to produce large pore fibrous and spherical SBA-15 particles. The effects of synthesis conditions on particle properties are presented. Large pore Spherical ordered SBA-15 materials were used to demonstrate for the first time the size-selective separation of proteins. BSA and lysozyme were tagged with fluorescent molecules, allowing direct visualization of the size selective separation of these proteins. Flow microcalorimetry (FMC) results were used to interpret the size-selective behavior of these materials.
520 $a The potential of siliceous SBA-15 materials to serve as hosts for enzymes in biocatalytic transformations was also explored. Materials with different pore sizes were used to study the effects of pore size and surface curvature on lipase activity. The synthesis and characterization of SBA-15 functionalized with amine and sulfonic groups is reported. Functionalized SBA-15 can be effectively used to selectively adsorb and desorb proteins based on ion exchange and hydrophobic interactions. Unusually high catalytic activity was observed for lipase immobilized on sulfonic SBA-15; FMC measurements for lipase immobilization suggested that structural rearrangements of lipase were responsible for this effect.
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650 4 $a Engineering, Chemical. $3 1018531
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710 2 $a University of Cincinnati. $3 960309
773 0 $t Dissertation Abstracts International $g 69-02B.
790 $a 0045
790 1 0 $a Pinto, Neville G., $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3302692