Item

Stability of bovine lactoferrin in luminal extracts and mucosal homogenates from rat intestine: a prelude to oral absorption

Yao, X
Bunt, Craig
Cornish, J
Quek, S-Y
Wen, J
Date
2014-12
Type
Journal Article
Fields of Research
ANZSRC::070710 Veterinary Pharmacology , ANZSRC::110104 Medical Biochemistry: Lipids , ANZSRC::110106 Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics) , ANZSRC::3101 Biochemistry and cell biology , ANZSRC::3404 Medicinal and biomolecular chemistry
Abstract
Oral delivery is the most common method for bovine lactoferrin (bLf) administration. However, the presence of proteolytic enzymes in the stomach and intestine limits the effective absorption of bLf within the gastrointestinal (GI) tract. To determine the extent of bLf proteolysis, several digestion models were developed using luminal extracts and mucosal homogenates isolated from four regions of rat intestine: duodenum, jejunum, ileum, and proximal colon. The kinetics of bLf degradation followed a pseudo-first-order rate, and almost complete hydrolysis of bLf was observed in the luminal extracts, indicating that bLf is more susceptive to luminal peptidases rather than mucosal enzymes. Moreover, a significant reduction in bLf proteolysis was observed in the presence of soybean trypsin inhibitor (SBTI), bestatin, and bacitracin, suggesting that there exist trypsin-like and aminopeptidase-like proteases, which play a key role in the degradation of bLf in the intestine. Lactoferrin was then encapsulated in several lipid-based delivery systems including liposomes and solid lipid particles (SLPs) with polymer modification, showing at least 50% of intact bLf remaining after 6 h of digestion compared with native bLf. These findings suggest that particle encapsulation may modulate protein digestion and possibly achieve sufficient oral bioavailability of bLf.
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© 2014 John Wiley & Sons A/S
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