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.)

ISBN 10: 3838323548 / ISBN 13: 9783838323541

Published by LAP LAMBERT Academic Publishing, 2010

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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 | Krishnan Sankaran (u. a.) | Taschenbuch | 208 S. | Englisch | 2010 | LAP LAMBERT Academic Publishing | EAN 9783838323541 | Verantwortliche Person für die EU: BoD - Books on Demand, In de Tarpen 42, 22848 Norderstedt, info[at]bod[dot]de | Anbieter: preigu Print on Demand.

Seller Inventory # 101386125

Bibliographic Details

• Title: Enzyme technology using Bacterial lipid modification enzyme LGT | Characterization of LGT with a new generic peptide assay and LGT-bioreactor prototype for lipopeptide synthesis
• Publisher: LAP LAMBERT Academic Publishing
• Publication Date: 2010
• Language: English
• ISBN 10: 3838323548
• ISBN 13: 9783838323541
• Binding: Taschenbuch
• Condition: Neu
• Dimensions: 220W x 150H x 14D millimeters 220 millimeters width by 150 millimeters height by 14 millimeters depth
• Weight: 328 grams
• Seller catalogs:
  • Bücher

About this title

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.