sankaran krishnan (13 Ergebnisse)

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Taschenbuch. Zustand: Neu. Enzyme technology using Bacterial lipid modification enzyme LGT | Characterization of LGT with a new generic peptide assay and LGT-bioreactor prototype for lipopeptide synthesis | Krishnan Sankaran (u. a.) | Taschenbuch | 208 S. | Englisch | 2010 | LAP LAMBERT Academic Publishing | EAN 9783838323541 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.

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Taschenbuch. Zustand: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Covalent lipid modification of proteins anchors hydrophilic proteins/peptides to hydrophobic surfaces and aid efficient performance in aqueous conditions as required in many biotechnological applications like ELISA, biosensors, targeted-drug delivery and liposomal integration. Lipid modification studied by him in bacteria extended the possibility of in vitro lipid modification, particularly for peptides. In this thesis the first enzyme of the pathway, phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt), which catalyzes the bulk of the lipidation has been utilized in devising a small bioreactor prototype for in vitro peptide modification. To achieve this, a new generic synthetic peptide assay was designed and used for its kinetic characterization and enrichment. The packed bed reactor with continuous and total feed-back operation in batch mode converted 65% of the model hydrophilic peptide substrate to lipopeptide. The higher conversion rate achieved in this study demonstrated the feasibility of such a bioreactor for lipid modification of a variety of peptides for potential biotech applications. 208 pp. Englisch.

Zustand: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Sankaran KrishnanA doctorate in Biochemistry from University of Hyderabad Prof. Sankaran joined USUHS,USA as PDF in 1990 and discovered the bacterial lipid modification pathway. From 1995 onwards at Anna University, he continues on i.

Taschenbuch. Zustand: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Covalent lipid modification of proteins anchors hydrophilic proteins/peptides to hydrophobic surfaces and aid efficient performance in aqueous conditions as required in many biotechnological applications like ELISA, biosensors, targeted-drug delivery and liposomal integration. Lipid modification studied by him in bacteria extended the possibility of in vitro lipid modification, particularly for peptides. In this thesis the first enzyme of the pathway, phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt), which catalyzes the bulk of the lipidation has been utilized in devising a small bioreactor prototype for in vitro peptide modification. To achieve this, a new generic synthetic peptide assay was designed and used for its kinetic characterization and enrichment. The packed bed reactor with continuous and total feed-back operation in batch mode converted 65% of the model hydrophilic peptide substrate to lipopeptide. The higher conversion rate achieved in this study demonstrated the feasibility of such a bioreactor for lipid modification of a variety of peptides for potential biotech applications.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 208 pp. Englisch.

Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Covalent lipid modification of proteins anchors hydrophilic proteins/peptides to hydrophobic surfaces and aid efficient performance in aqueous conditions as required in many biotechnological applications like ELISA, biosensors, targeted-drug delivery and liposomal integration. Lipid modification studied by him in bacteria extended the possibility of in vitro lipid modification, particularly for peptides. In this thesis the first enzyme of the pathway, phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt), which catalyzes the bulk of the lipidation has been utilized in devising a small bioreactor prototype for in vitro peptide modification. To achieve this, a new generic synthetic peptide assay was designed and used for its kinetic characterization and enrichment. The packed bed reactor with continuous and total feed-back operation in batch mode converted 65% of the model hydrophilic peptide substrate to lipopeptide. The higher conversion rate achieved in this study demonstrated the feasibility of such a bioreactor for lipid modification of a variety of peptides for potential biotech applications.

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