Importance of phospholipids, pancreatic phospholipase A2, and fatty acid for the digestion of dietary fat

Borgström, Bengt

doi:10.1016/0016-5085(80)90777-5

Cited by 159 publications

(61 citation statements)

References 16 publications

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“…The importance of PC hydrolysis in facilitating intestinal lipid digestion and absorption has been well demonstrated in studies using intestinal cells and enzymes in vitro [15 -19] and in our study using a rat model in vivo with lymph cannula [39]. Since PC is present on the surface of lipid emulsions, the outer coat of PC hinders the hydrolysis of the core TG by pancreatic lipase, whereas even a limited hydrolysis of PC by pancreatic PLA 2 facilitates the binding of lipase/colipase to the substrate interface and results in a rapid hydrolysis of TG [15,40,41]. In studies using a rat intestinal cell line [42], pancreatic lipase/colipase was shown to be ineffective in hydrolyzing TG that was incorporated into PC-containing lipid emulsions, and the initial hydrolysis of the surface PC by pancreatic PLA 2 significantly increased the hydrolysis of TG by pancreatic lipase/colipase.…”

Section: Discussionmentioning

confidence: 50%

Green tea catechins inhibit pancreatic phospholipase A2 and intestinal absorption of lipids in ovariectomized rats

Wang

Noh

Koo

2006

The Journal of Nutritional Biochemistry

104

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Section: Discussionmentioning

confidence: 50%

Green tea catechins inhibit pancreatic phospholipase A2 and intestinal absorption of lipids in ovariectomized rats

Wang

Noh

Koo

2006

The Journal of Nutritional Biochemistry

104

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“…This clearly demonstrates that the effect of PL on PTL activity occurs even in the presence of COL. The presence of PL at the interface inhibits the binding of the PTL-COL complex, as previously reported [7]. However, the inhibitory effect of PL on either PTL alone or the PTL-COL complex depends heavily on the amount of incorporated PL at the oil-water interface.…”

Section: Lipid Hydrolysismentioning

confidence: 62%

“…Reportedly, the interfacial adsorption of PTL is sterically inhibited by the head groups of PL [18]. However, this inhibition is overcome in the presence of PLA 2 [7].…”

Section: Introductionmentioning

confidence: 99%

Changes in WPI-Stabilized Emulsion Interfacial Properties in Relation to Lipolysis and ß-Carotene Transfer During Exposure to Simulated Gastric–Duodenal Fluids of Variable Composition

2010

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A whey protein isolate-stabilized oil-in-water emulsion was investigated as a carrier for β-carotene (BC). The changes in emulsion structure during gastric and upper intestinal digestion and BC transfer to the mixed bile salt micelles were studied using a comprehensive in vitro procedure which included colipase (COL), phospholipids (PL), and phospholipase A 2 (PLA 2 ), in addition to the standard enzymes and bile salts (BS). During the gastric phase, peptic hydrolysis of the proteins adsorbed at the interface resulted in droplet destabilization. Changes in droplet size distribution continued in the duodenal phase, in the presence of BS alone or BS and PL (BS-PL). Marked influences of BS, COL, PL, and PLA 2 on pancreatic triglycerides lipase (PTL) activity were observed. While both BS and PL inhibited PTL activity, the presence of COL and PLA 2 minimized the inhibition by BS and PL, respectively. The optimal PTL activity (72.3±1.7% lipid hydrolysis) was only achievable with the inclusion of COL and PLA 2 , although these components are rarely included in in vitro digestion models. The efficiency of BC micellization was 31.2±1.1% in the presence of only BS and no significant differences were observed in the case of the BS-PL or BS-PL-COL systems (p>0.05). However, more BC was micellarized (48.5±0.9%) in the presence of BS-PL-COL-PLA 2 (p<0.05). The extent of BC micellarized was linearly proportional to the extent of lipid hydrolysis. These results contribute to an understanding of how emulsions can be used to encapsulate and deliver lipophilic bioactive molecules. Furthermore, they underscore the importance of using physiologically relevant in vitro models to study lipid hydrolysis and the release and transfer of encapsulated molecules.

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“…In vitro digestion of human milk fat globules or of synthetic fat emulsions containing phospholipid and triglyceride proceeds most efficiently with a mixture of lipases [164][165][166]. The inclusion of both CEL and PTL in a model system doubled the rate obtained with PTL alone, suggesting that CEL may preferentially act on products of PTL digestion [167].…”

Section: Animal Studiesmentioning

confidence: 94%

Human Pancreatic Digestive Enzymes

2007

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A primary function of the pancreas is to produce digestive enzymes that are delivered to the small intestine for the hydrolysis of complex nutrients. Much of our understanding of digestive enzymes comes from studies in animals. New technologies and the availability of the sequence of the human genome allow for a critical review of older reports and assumptions based on animal studies. This report updates our understanding of human pancreatic digestive enzymes with a focus on new insights into the biology of human proteases, lipases and amylases.

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Importance of phospholipids, pancreatic phospholipase A2, and fatty acid for the digestion of dietary fat

Cited by 159 publications

References 16 publications

Green tea catechins inhibit pancreatic phospholipase A2 and intestinal absorption of lipids in ovariectomized rats

Green tea catechins inhibit pancreatic phospholipase A2 and intestinal absorption of lipids in ovariectomized rats

Changes in WPI-Stabilized Emulsion Interfacial Properties in Relation to Lipolysis and ß-Carotene Transfer During Exposure to Simulated Gastric–Duodenal Fluids of Variable Composition

Human Pancreatic Digestive Enzymes

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