Introduction. The standard porcine-derived pancreatic enzyme replacement therapy (PERT) is a lifesaving treatment for
patients with diseases causing exocrine pancreatic insufficiency (EPI). An attempt to replace PERT with microbial enzymes
were undertaken. The aim was to highlight whether the mode of application, mixed with food or applied directly to the
stomach, of pancreatic-like enzymes of microbial origin (PLEM) can affect their activity along the gastrointestinal tract.
Materials and method. The activity of amylase, lipase and proteinase in the stomach, duodenum and ileum were tested
in EPI pigs (n=6) after supplementation of PLEM, either orally – before and during feed consumption – or via the stomach –
before and during feed consumption. Healthy pigs not treated with PLEM (n=3) served as controls. Activity of the enzymes
measured in the chyme were obtained together with the digesta pH. Activity of the enzymatic residues in the stool samples
was also checked.
Results. The highest pancreatic enzyme activities were found in the duodenum of the healthy pigs (amylase 162,68 kU/
mL, lipase 507,34 kU/mL and protolitic (trypsin) activity 357,60 kU/mL). Nevertheless, the microbial enzymes remained also
active along the entire length of the GIT – including stomach in EPI pigs, regardless of their route of administration. However,
activity level was significantly lower.
Discussion. Results indicate that the activity pattern of PLEM in the small intestine mimics the activity of the natural
endogenous pancreatic enzymes in healthy pigs. The most physiological features of PLEM were observed when enzymes
were offered orally. The magnitude of PLEM activity in the stomach of EPI pigs was essential and significantly higher than
that measured in healthy pigs, thus being somewhat not physiological, and for health reasons of the patients should be
further explored. Interestingly, specific trypsin-like activity was measured in all parts of the GIT after PLEM application.
However, proteolytic activity of the experimental proteaze in in vitro studies did not exhibit trypsin-like activity.
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