Esterase, from pig liver, namely carboxylesterase, is responsible for the hydrolysis of carboxylesters into the corresponding alcohol and carboxylic acid. Esterase is principally expressed in tissues that maintain a barrier function, including the epithelia of the lung and gut, liver, kidney and skin[1]. Esterase is commonly used in vitro to verify whether esterases can hydrolyze or activate substrates, probes, or prodrugs. Esterase from porcine liver (0-25pg; 0-625amol) is used as a standard enzyme, with Fluorescein diacetate (FDA) as the fluorescent substrate, to establish a standard curve for esterase activity and to detect esterase activity in BY-2 tobacco cells and spruce embryogenic cells[2]. Esterase (10µL; 1.66U/µL) is used to pretreat the synthesized probe for 3.5h to induce de-esterification in advance and evaluate changes in background fluorescence[3].
References:
[1] Hatfield MJ, Umans RA, Hyatt JL, et al. Carboxylesterases: General detoxifying enzymes. Chem Biol Interact. 2016;259(Pt B):327-331.
[2] Vitecek J, Petrlova J, Adam V, Havel L, Kramer KJ, Babula P, Kizek R. A Fluorimetric Sensor for Detection of One Living Cell. Sensors. 2007; 7(3):222-238.
[3] Watkins RW, Lavis LD, Kung VM, Los GV, Raines RT. Fluorogenic affinity label for the facile, rapid imaging of proteins in live cells. Org Biomol Chem. 2009;7(19):3969-3975.