Part:BBa_K4949001
Thermoanaerobacter thermohydrosulfuricus lipase (TTL)
Thermoanaerobacter thermohydrosulfuricus lipase (TTL) is a thermophilic lipase that has been studied in the potential degradation of polyethylene terephthalate (PET). This protein expresses well in E.coli and sufficient quantity can be purified by IMAC test is ability to cleave ester linkages.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Figure 1. Michaelis-Menten Esterase Activity Assay of MGS0156 with 4-nitrophenyl octanoate (NPO). Assays were conducted with 1.5 µM of lipase in PBS with NPO concentration ranging from 0.0365-0.11 µM. The rate of change in absorbance was monitored at 410 nm for 1 min. A) Wild type MGS0156 chromogenic assay with initial rate as a function of substrate concentration at 25 ℃ B) Wild type MGS0156 chromogenic assay with initial rate as a function of substrate concentration at 60 ℃ C) MGS0156 chromogenic assay with initial rate as a function of substrate concentration, with norleucine introduced by residue specifically by SPI at 25 ℃
Figure 2. Michaelis-Menten Esterase Activity Assay of MGS0156 with 4-nitrophenyl butyrate (pNOB). Assays were conducted with 1.5 µM of lipase in PBS with pNOB concentration ranging from 0.0365 - 0.11 µM. The rate of change in absorbance was monitored at 410 nm for 1 min. A) Wild-type MGS0156 chromogenic assay with initial rate as a function of substrate concentration at 25 degrees C. B) Wild-type MGS0156 chromogenic assay with initial rate as a function of substrate concentration at 60 ℃. C) MGS0156 chromogenic assay with initial rate as a function of substrate concentration, with norleucine introduced by residue specifically by SPI at 25℃.
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