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Refolding of denatured lysozyme assisted by artificial chaperones in reverse micelles

Paper ID Volume ID Publish Year Pages File Format Full-Text
5028 271 2006 4 PDF Available
Title
Refolding of denatured lysozyme assisted by artificial chaperones in reverse micelles
Abstract

This article reports oxidative protein refolding assisted by artificial chaperones in reverse micelles formed by nonionic surfactant of sorbitan trioleate modified with Cibacron Blue F-3GA in n-hexane. The denatured/reduced lysozyme was used as a model protein and cetyltrimethylammonium bromide (CTAB) and β-cyclodextrin as the artificial chaperones. The use of the artificial chaperones has proved to increase the refolding efficiency of denatured–reduced lysozyme at the concentration range studied (3.5–5.9 mg/mL). Moreover, the artificial chaperones increased the refolding yield in a wide range of urea concentrations. However, the optimal urea concentration range was little affected by the presence of the artificial chaperones.

Keywords
Protein refolding; Lysozyme; Reverse micelles; Artificial chaperone; Nonionic surfactant; Cibacron Blue F-3GA
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Refolding of denatured lysozyme assisted by artificial chaperones in reverse micelles
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 31, Issue 1, 1 August 2006, Pages 92–95
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
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