[1] However, due to the unique characteristics of lingual lipase, including a pH optimum 4.5–5.4 and its ability to catalyze reactions without bile salts, the lipolytic activity continues through to the stomach.

Lingual lipase uses a catalytic triad consisting of aspartic acid-203 (Asp), histidine-257 (His), and serine-144 (Ser), to initiate the hydrolysis of a triglyceride into a diacylglyceride and a free fatty acid.

It has, thus, been proposed that a possible treatment option for exocrine pancreatic insufficiency would be enzyme replacement therapy using lingual lipase, increasing the amount of dietary fat absorption and decreasing the risk of malnutrition.

The proposed mechanism of lingual lipase preferentially cleaving short and medium chain triacylglycerols provides a means for absorption without the need for micelle formation and chylomicrons.

Short and medium chain free fatty acids can be absorbed directly through the mucosal cells into the blood stream without further packaging and hence play a crucial role in nutrition for CF patients (and neonates).

This fact, in combination with the bile salt deficiency and low pH throughout the gastrointestinal tract of the neonate, demands that lingual lipase be the main enzyme catalyzing the hydrolysis of dietary fat.