Porcine pancreatic lipase related protein 2 has high triglyceride lipase activity in the absence of colipase

Xunjun Xiao, Leah E. Ross, Wednesday A. Sevilla, Yan Wang, Mark E. Lowe

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Efficient dietary fat digestion is essential for newborns who consume more dietary fat per body weight than at any other time of life. Inmanymammalian newborns, pancreatic lipase related protein 2 (PLRP2) is the predominant duodenal lipase. Pigs may be an exception since PLRP2 expression has been documented in the intestine but not in the pancreas. Because of the differences in tissue-specific expression, we hypothesized that the kinetic properties of porcine PLRP2 would differ from those of othermammals. To characterize its properties, recombinant porcine PLRP2 was expressed in HEK293T cells and purified to homogeneity. Porcine PLRP2 had activity against tributyrin, trioctanoin and triolein. The activity was not inhibited by bile salts and colipase, which is required for the activity of pancreatic triglyceride lipase (PTL), minimally stimulated PLRP2 activity. Similar to PLRP2 from other species, PLRP2 from pigs had activity against galactolipids and phospholipids. Importantly, porcine PLRP2 hydrolyzed a variety of dietary substrates including pasteurized human mother's milk and infant formula and its activitywas comparable to that of PTL. In conclusion, porcine PLRP2 has broad substrate specificity and has high triglyceride lipase activity even in the absence of colipase. The data suggest that porcine PLRP2 would be a suitable lipase for inclusion in recombinant preparations for pancreatic enzyme replacement therapy.

Original languageEnglish
Pages (from-to)1435-1441
Number of pages7
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Issue number9
StatePublished - 2013


  • Colipase
  • Galactolipid
  • Lipase
  • Phospholipid
  • Triglyceride


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