Activity of recombinant GST in Escherichia coli grown on glucose and glycerol |
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| Institution: | 1. Université Paris-Est, LEESU (UMR MA 102), UPEC, UPEMLV, ENPC, AgroParisTech, 94010 Créteil, France;2. Laboratoire LGCIE, Université de Lyon, INSA-Lyon, Bât. Carnot, 9 rue de la Physique, 69621 Villeurbanne, France;3. Université Européenne de Bretagne, Rennes, France;4. Université de Bretagne Occidentale, IUEM, Lemar, UMR CNRS 6539, rue Dumont D''Urville, 29280 Plouzané, France |
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| 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. |
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