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Time course of gastric lipase activity in extracts kept at 20 • C, at pH 2.2 (circles) or at pH 5 (triangles). The extracts were placed in new tubes on day 14. Bars are confidence intervals (0.95; n = 6).
Source publication
The properties of recombinant human gastric lipase produced in Arabidopsis thaliana roots have been investigated with the goal of determining the potential of the enzyme. This enzyme is stably bound to roots and can be extracted using a buffer at pH 2.2. This enzyme retains over 75% of its activity after two weeks at room temperature when stored in...
Contexts in source publication
Context 1
... pHs were chosen because they are the pH of the extraction buffer and of the assay buffer, respectively. Whereas extracts at pH 2.2 retained approximately 75% of lipase activity after 14 days, those at pH 5 lost over 50% activity over the same time span (Figure 2). Transferring the diluted solutions of lipase to new tubes on day 14 resulted in a sharp drop of lipase activity after 24 h, especially at pH 5. To test for adsorption on tubes, lipase diluted in solutions at pH 2.2 or at pH 5 were placed in tubes for 24 h and removed. ...
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Citations
... Apart from the extensive body of research dedicated to exploring bioactive small molecules derived from plants, a notable study by Dr. Guerineau reported the successful production of recombinant human gastric lipase by Arabidopsis thaliana root culture while also providing a comprehensive characterization of the enzyme's properties [13]. This investigation showcases the application of molecular pharming in plants as a means to synthesize recombinant proteins, which are big molecules. ...
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