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In vitro refolding of PEGylated lipase

Paper ID Volume ID Publish Year Pages File Format Full-Text
25160 43556 2007 3 PDF Available
Title
In vitro refolding of PEGylated lipase
Abstract

Covalent modification of proteins with polyethylene glycol (PEG) has become a well established drug enhancement strategy in the biopharmaceutical industry. The general benefits of PEGylation, such as prolonged serum half-lives or reduced in vivo immunogenicity, are well known. To date, the PEGylation process has been performed with purified proteins, which often requires additional multi-step purification steps to harvest the desired PEGylate. However, it would be beneficial for bioprocessing if ‘renaturation,’ i.e. in vitro refolding and ‘modification,’ and PEGylation can be integrated, especially for inclusion body proteins. We investigated the feasibility of protein PEGylation under denaturing conditions and of protein refolding with the attached PEG molecule. Using lipase as a model protein, PEGylation occurred in 8 M urea and covalently attached PEG did not appear to hinder subsequent refolding.

Keywords
PEGylation; PEGylated lipase; Refolding; Integrated process
First Page Preview
In vitro refolding of PEGylated lipase
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 131, Issue 2, 31 August 2007, Pages 177–179
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering