Carboxyl ester lipase (bile salt-stimulated lipase), colipase, lipase, and phospholipase A2 levels in pancreatic enzyme supplements

Scand J Gastroenterol. 1997 Mar;32(3):261-7. doi: 10.3109/00365529709000204.

Abstract

Background: Pancreatic lipolytic activity originates from lipase (LIP) and its cofactor colipase (COL), carboxyl ester lipase (CEL), and phospholipase A2 (PLA2). Yet there are few data on the levels of individual lipolytic enzymes in pancreatic enzyme supplements (PES). This study determines activity and immunoreactive mass in some commonly used PES and thus contributes to the understanding of the poor relationship between 'lipase dose' and clinical improvements.

Methods: Recommended doses of each PES were incubated at 37 degrees C for 2 h in a 1-mM Tris-maleate buffer, pH 7.0, containing 150 mM NaCl and 1 mM CaCl2. Aliquots for determinations of enzyme activities and for immunochemical mass were taken every half hour. For comparison a standard dose was defined as 10,000 declared lipase units.

Results: No simple parallelism between LIP, COL, CEL, and/or PLA2 activities was seen. The LIP contents ranged from 135% to 301% of the standard dose. None of the PES were short of COL (227%-504%). The variation in CEL was twentyfold, and in PLA2 sevenfold. Less variations were seen in the mass composition. There was considerable variation in activity to mass ratios (particularly for CEL), declared lipase units per recommended dose (6000-160,000), and cost (0.36-3.52 SEK).

Conclusions: PES differ considerably in their content of lipolytic enzymes. CEL activities were relatively low and COL and PLA2 activities high compared with normal duodenal content. The manufacturing procedure can be improved to increase the lipolytic activity in PES in a broader meaning. It seems to be most important to increase the amount of CEL. From these in vitro data we advocate a more careful decision in the choice of PES for each patient, depending on the total clinical picture. Money can be saved without disadvantage to the patient.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carboxylesterase
  • Carboxylic Ester Hydrolases / analysis
  • Colipases / analysis
  • Drug Combinations
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / therapeutic use
  • Humans
  • Lipase / analysis
  • Pancreatic Extracts / chemistry*
  • Pancreatic Extracts / therapeutic use
  • Pancreatin / chemistry
  • Pancreatin / therapeutic use
  • Peptide Hydrolases / chemistry
  • Peptide Hydrolases / therapeutic use
  • Phospholipases A / analysis
  • Phospholipases A2
  • Radioimmunoassay

Substances

  • Colipases
  • Drug Combinations
  • Pancreatic Extracts
  • festal
  • Pancreatin
  • Combizym
  • Carboxylic Ester Hydrolases
  • Carboxylesterase
  • Lipase
  • Phospholipases A
  • Phospholipases A2
  • Glycoside Hydrolases
  • Peptide Hydrolases