This thesis deals with the preparation microparticles by spray-freeze-drying (SFD). As the process consists of various unit operations, the stability of labile APIs, such as proteins, can be serverly impaired. The secondary structure of a protein is known to be directly linked to its overall stability. However, quantification of protein secondary structure by FTIR spectroscopy can show poor reproducibility. Therefore, the first part of this thesis covers the development of a new FTIR method for objective and fast determination of protein secondary structure. The second part investigates the influence of atomization conditions on protein secondary and tertiary structure as well as residual enzyme activity during SFD. The process is analyzed after a) atomization b) atomization, freezing and thawing and c) the complete SFD process. A thorough comparison of the utilized ultrasound nozzles (including particle size distribution, temperatures and cavitation effects) is performed in the third part of this thesis. In the fourth and last part, different formulations containing a mixture of alpha-chymotrypsin and various excipients are evaluated for their stability.
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This thesis deals with the preparation microparticles by spray-freeze-drying (SFD). As the process consists of various unit operations, the stability of labile APIs, such as proteins, can be serverly impaired. The secondary structure of a protein is known to be directly linked to its overall stability. However, quantification of protein secondary structure by FTIR spectroscopy can show poor reproducibility. Therefore, the first part of this thesis covers the development of a new FTIR method for objective and fast determination of protein secondary structure. The second part investigates the influence of atomization conditions on protein secondary and tertiary structure as well as residual enzyme activity during SFD. The process is analyzed after a) atomization b) atomization, freezing and thawing and c) the complete SFD process. A thorough comparison of the utilized ultrasound nozzles (including particle size distribution, temperatures and cavitation effects) is performed in the third part of this thesis. In the fourth and last part, different formulations containing a mixture of alpha-chymotrypsin and various excipients are evaluated for their stability.
Sebastian Vonhoff passed his licensing exam as German pharmacist in 2006. From 2006 - 2009 he did his PhD thesis under the supervision of Prof. Dr. Geoffrey Lee at the Division of Pharmaceutics (University Erlangen-Nuremberg). Focus laid on analysis of protein secondary structure by FTIR spectroscopy and particle formation by spray-freeze-drying.
Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.
Vendeur : BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -This thesis deals with the preparation microparticles by spray-freeze-drying (SFD). As the process consists of various unit operations, the stability of labile APIs, such as proteins, can be serverly impaired. The secondary structure of a protein is known to be directly linked to its overall stability. However, quantification of protein secondary structure by FTIR spectroscopy can show poor reproducibility. Therefore, the first part of this thesis covers the development of a new FTIR method for objective and fast determination of protein secondary structure. The second part investigates the influence of atomization conditions on protein secondary and tertiary structure as well as residual enzyme activity during SFD. The process is analyzed after a) atomization b) atomization, freezing and thawing and c) the complete SFD process. A thorough comparison of the utilized ultrasound nozzles (including particle size distribution, temperatures and cavitation effects) is performed in the third part of this thesis. In the fourth and last part, different formulations containing a mixture of alpha-chymotrypsin and various excipients are evaluated for their stability. 188 pp. Englisch. N° de réf. du vendeur 9783838117713
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Vendeur : moluna, Greven, Allemagne
Etat : New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Vonhoff SebastianSebastian Vonhoff passed his licensing exam as German pharmacistin 2006. From 2006 - 2009 he did his PhD thesis under thesupervision of Prof. Dr. Geoffrey Lee at the Division ofPharmaceutics (University Erlangen-Nure. N° de réf. du vendeur 5406127
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Vendeur : preigu, Osnabrück, Allemagne
Taschenbuch. Etat : Neu. Microparticle Formation by Spray-Freeze-Drying | The Influence of Atomization Conditions on Protein Secondary and Tertiary Structure | Sebastian Vonhoff | Taschenbuch | 188 S. | Englisch | 2015 | Südwestdeutscher Verlag für Hochschulschriften | EAN 9783838117713 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu. N° de réf. du vendeur 101045724
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Vendeur : buchversandmimpf2000, Emtmannsberg, BAYE, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - Print on Demand Titel. Neuware -This thesis deals with the preparation microparticles by spray-freeze-drying (SFD). As the process consists of various unit operations, the stability of labile APIs, such as proteins, can be serverly impaired. The secondary structure of a protein is known to be directly linked to its overall stability. However, quantification of protein secondary structure by FTIR spectroscopy can show poor reproducibility. Therefore, the first part of this thesis covers the development of a new FTIR method for objective and fast determination of protein secondary structure. The second part investigates the influence of atomization conditions on protein secondary and tertiary structure as well as residual enzyme activity during SFD. The process is analyzed after a) atomization b) atomization, freezing and thawing and c) the complete SFD process. A thorough comparison of the utilized ultrasound nozzles (including particle size distribution, temperatures and cavitation effects) is performed in the third part of this thesis. In the fourth and last part, different formulations containing a mixture of alpha-chymotrypsin and various excipients are evaluated for their stability.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 188 pp. Englisch. N° de réf. du vendeur 9783838117713
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Vendeur : AHA-BUCH GmbH, Einbeck, Allemagne
Taschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - This thesis deals with the preparation microparticles by spray-freeze-drying (SFD). As the process consists of various unit operations, the stability of labile APIs, such as proteins, can be serverly impaired. The secondary structure of a protein is known to be directly linked to its overall stability. However, quantification of protein secondary structure by FTIR spectroscopy can show poor reproducibility. Therefore, the first part of this thesis covers the development of a new FTIR method for objective and fast determination of protein secondary structure. The second part investigates the influence of atomization conditions on protein secondary and tertiary structure as well as residual enzyme activity during SFD. The process is analyzed after a) atomization b) atomization, freezing and thawing and c) the complete SFD process. A thorough comparison of the utilized ultrasound nozzles (including particle size distribution, temperatures and cavitation effects) is performed in the third part of this thesis. In the fourth and last part, different formulations containing a mixture of alpha-chymotrypsin and various excipients are evaluated for their stability. N° de réf. du vendeur 9783838117713
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