Production and Potential Applications of Recombinant Gastric Lipases in Biotechnology
Gastric lipases have been purified either from gastric juice or from fundic gastric mucosae and characterized in vitro. HGL was first purified by Trruppathi and Balasubramanian (1982) and its secretion was stimulated by injecting pentagastrin (Szafran et al., 1978, Moreau et al., 1988). Nowadays, the enzyme is purified using cation-exchange (Mono S) chromatography followed by an immunoaffinity column procedure using monoclonal antibodies. Lipase activity can be measured potenti~ metrically on short<hain (tributyroylglycerol, TC4), medium-chain (trioctanoylglycerol, TC8) and long<hain (lntralipid™) triacylglycerols at 37°C using a pH-stat (Gargouri et al., 1986). The maximum specific activities are 1160 units/mg at pH 6, Ill 0 units/mg at pH 6 and 600 units/mg at pH 5, on TC4, TC8 and IntralipidTM, respectively.