Lipolysis of the semi-solid self-emulsifying excipient Gelucire® 44/14 by digestive lipases

We studied the lipolysis of Gelucire® 44/14 by porcine pancreatic extracts, human pancreatic juice and several purified digestive lipases

Sylvie Fernandez

2008

Scholarcy highlights

  • Gelucire® 44/14 is a semi-solid self-emulsifying excipient used for the oral delivery of poorly water-soluble drugs
  • Human pancreatic lipase, the main lipase involved in the digestion of triacylglycerols, did not show any significant activity on Gelucire® 44/14 or on either of its individual compounds, C8-C18 acylglycerols and PEG-32 esters
  • We compared the lipolysis of Gelucire® 44/14 with that of Labrasol®, another self-emulsifying excipient, which is liquid at room temperature
  • Human pancreatic juice showed similar rates of activity on both Gelucire® 44/14 and Labrasol®. This finding means that these excipients are hydrolyzed in vivo during pancreatic digestion, mainly by Carboxyl ester hydrolase in the case of Gelucire® 44/14 and by both human pancreatic lipase-related protein 2 and CEH in that of Labrasol®, whereas HPL showed very low activities on each of these two excipients
  • This is the first time the effects of PEG and acyl chain length on the lipolytic activity of digestive lipases on PEG esters have been investigated

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