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Activity of recombinant GST in Escherichia coli grown on glucose and glycerol

Paper ID Volume ID Publish Year Pages File Format Full-Text
35825 45108 2007 5 PDF Available
Title
Activity of recombinant GST in Escherichia coli grown on glucose and glycerol
Abstract

We have investigated production, solubility and activity of recombinant glutathione-S-transferase (GST) expressed in Escherichia coli BL21 grown in defined media with glucose or glycerol as carbon source. GST was predominantly expressed as a soluble protein on both carbon sources, and 83–84% was found in the supernatant after cell lysis. In cultures grown on glucose, only 32 ± 9% of the GST was active, while 76 ± 13% of the GST was active in cultures grown on glycerol. This shows that glycerol has the potential to increase the activity of soluble GST in E. coli cultures in vivo.

Keywords
E. coli; Glutathione-S-transferase; Glycerol; Activity
First Page Preview
Activity of recombinant GST in Escherichia coli grown on glucose and glycerol
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 42, Issue 8, August 2007, Pages 1259–1263
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering