Novel potential of pancreatic-like enzymes of microbial origin in exocrine pancreatic insufficiency – study on a pig model
Journal Title: Journal of Pre-Clinical and Clinical Research - Year 2015, Vol 9, Issue 1
Abstract
[b]Introduction.[/b] 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. [b]Materials and method[/b]. 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. [b]Results[/b]. 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. [b]Discussion.[/b] 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.
Authors and Affiliations
Katrin Szwiec, Kateryna Goncharova, Jose Luis Valverde-Piedra , Galyna Ushakova, Tetiana Kovalenko, Iryna Osadchenko, Marek Kardas, Paulina Świeboda, Paweł Podgurniak, Mateusz Winiarczyk, Elżbieta Grochulska-Niedworok, Liudmila Lozinska, Rafał Filip, Stefan G Pierzynowski
Keywords
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