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Enzyme technology using Bacterial lipid modification enzyme LGT: Characterization of LGT with a new generic peptide assay and LGT-bioreactor prototype for lipopeptide synthesis - Couverture souple

Sankaran, Krishnan

 
9783838323541: Enzyme technology using Bacterial lipid modification enzyme LGT: Characterization of LGT with a new generic peptide assay and LGT-bioreactor prototype for lipopeptide synthesis
Couverture souple
ISBN 10 : 3838323548 ISBN 13 : 9783838323541
Editeur : LAP Lambert Academic Publishing, 2009

Synopsis

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.

Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.

Présentation de l'éditeur

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.

Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.

Éditeur
LAP Lambert Academic Publishing
Date d'édition
2009
Langue
anglais
ISBN 10 
3838323548
ISBN 13 
9783838323541
Reliure
Broché
Nombre de pages
208
Coordonnées du fabricant
non disponible
Personne responsable
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