Difference between revisions of "Part:BBa K1403015:Experience"
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We took advangage of this indole production activity to characterize the TMM enzyme. E. coli that were cultured in LB supplemented with tryptophan (2 g/L) produced a deep blue pigment with absorbance properties matching indigo (Fig. 1). Without TMM expression or without tryptophan, indigo production was minimal or absent. | We took advangage of this indole production activity to characterize the TMM enzyme. E. coli that were cultured in LB supplemented with tryptophan (2 g/L) produced a deep blue pigment with absorbance properties matching indigo (Fig. 1). Without TMM expression or without tryptophan, indigo production was minimal or absent. | ||
[[File:Spectrum_indigo.png|center|650px]] | [[File:Spectrum_indigo.png|center|650px]] | ||
| − | + | '' Average absorbances of DMSO extractions from bacterial lysates shows TMM activity.'' | |
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UNIQ2502997b49a4a83d-partinfo-00000000-QINU UNIQ2502997b49a4a83d-partinfo-00000001-QINU The TMM enzyme is not specific to TMA as a substrate. It is also known to oxidize indole to indoxyl, which dimerizes into the well known blue pigment indigo. Indole is a natural product of tryptophan metabolism in E. coli. We took advangage of this indole production activity to characterize the TMM enzyme. E. coli that were cultured in LB supplemented with tryptophan (2 g/L) produced a deep blue pigment with absorbance properties matching indigo (Fig. 1). Without TMM expression or without tryptophan, indigo production was minimal or absent.
Average absorbances of DMSO extractions from bacterial lysates shows TMM activity.