Abstract
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 a pH 2.2 buffer. Some of this activity loss was due to the adsorption of the enzyme to the surface of the container. There was no loss of lipase activity in dehydrated roots stored at room temperature for 27 months. The half-life of the enzyme was approximately 15 min when stored in solution at 60 °C whereas dried roots retained 90% lipase activity after one hour at 80 °C. In vitro binding assays using different root cell wall extracts suggested that the lipase was bound to pectin in the roots. Lipase released from the root powder hydrolyzed tributyrin. The high stability of the recombinant human gastric lipase makes this enzyme a good candidate to be tested as a catalyst, whether in solution or bound to roots.