Studies on the detergent inhibition of pancreatic lipase activity.

Gargouri, Youssef; Julien, Robert M.; Bois, A.; Verger, Robert; Sarda, Louis

doi:10.1016/s0022-2275(20)37884-6

Cited by 162 publications

(43 citation statements)

References 26 publications

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“…In real oils, these properties can be coupled, requiring independent measurements to identify the limiting process for each lipid. Bile salts are likely responsible, as they are known to control both the bulk solubilization 48,49 and the interfacial lipolysis 27,49,50 as a non-monotonous function of their concentration.…”

Section: Discussionmentioning

confidence: 99%

In vitro digestion of fish oils rich in n-3 polyunsaturated fatty acids studied in emulsion and at the oil–water interface

2013

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The in vitro digestion of β-lactoglobulin stabilized emulsions rich in the n-3 polyunsaturated fatty acids, eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), was studied using several physicochemical techniques. Artificial media for the mouth, stomach and small intestine were used in a sequential static in vitro digestion method. Different sizing techniques were compared to follow the droplet size during the digestion steps, including diffusing wave spectroscopy (DWS) which allowed direct measurements on undiluted emulsions. Titration of fatty acids confirmed that the digestion of such emulsified fish oils is partial. The study of the digestion at the oil-water interface using tensiometry revealed specific affinities between lipids and proteins. These could explain the emulsion and the single droplet lipolysis. Nevertheless, by comparing our results to a previous study on fish oil lipolysis, we identified two other important factors. Those were the aqueous solubility and the rate of hydrolysis of the individual fatty acids, the emulsion with the most soluble and hydrolysable ones being digested more quickly.

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Section: Discussionmentioning

confidence: 99%

In vitro digestion of fish oils rich in n-3 polyunsaturated fatty acids studied in emulsion and at the oil–water interface

2013

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“…Porcine pancreatic colipase (in the form of procolipase) was a gift from Prof. L. Sarda (Laboratoire de Chimie Biologique, Marseille, France). The specific activities of pancreatic lipase and colipase were measured titrimetrically using sta ndard assays previously described by Gargouri et al (16) and Rathelot et al (17 ) and were estimated to be 8000 and 10,000 units mg " ", respectively. Bovine serum albumin and anti-mouse immunoglobulin G conjugated to peroxidase or alkaline phosphatase wer e from Sigma.…”

Section: Methodsmentioning

confidence: 99%

Human Pancreatic Lipase

Aoubala¹,

Fournière²,

Douchet³

et al. 1995

Journal of Biological Chemistry

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Several monoclonal antibodies (mAbs) were prepared against human pancreatic lipase (HPL). Two enzyme-linked immunosorbent assay (ELISA) procedures were set up for screening hybridomas producing specific antibodies. Four mAbs (81-23, 146-40, 315-25, and 320-24) of the IgG1 isotype were found to react with HPL in both simple sandwich and double sandwich ELISAs, while mAb 248-31, of the IgG2b isotype, reacted only with HPL in a double sandwich ELISA. The results of Western blot analysis carried out with native and SDS-denatured HPLs indicated that mAb 248-31 recognized only native HPL, while all the other mAbs recognized both forms of HPL. Since mAb 248-31 did not recognize SDS-denatured HPL, it was not possible to localize its epitope. To carry out epitope mapping along the primary sequence of HPL, four fragments (14, 26, 30, and 36 kDa) resulting from a limited chymotryptic cleavage of HPL were characterized by Western blotting as well as N-terminal amino acid sequence analysis. Of the above five anti-HPL mAbs, four (81-23, 248-31, 315-25, and 320-24) were found to inhibit the lipolytic activity of HPL (in both the presence and absence of bile salts and colipase), while mAb 146-40 had no inhibitory effects. The epitope recognized by mAb 146-40 was found to be located in the N-terminal domain (Lys1-Phe335). Combined immunoinactivation and epitope mapping studies showed that three inhibitory mAbs (81-23, 315-25, and 320-24) recognize overlapping epitopes from the hinge region between the N- and C-terminal domains of HPL, belonging to the 26-kDa fragment. In the presence of lipids, a significant decrease has been observed in the bending angle between the N- and C-terminal domains of the HPL tertiary structure (van Tilbeurgh, H., Egloff, M. P., Martinez, C., Rugani, N., Verger, R. and Cambillau, C. (1993) Nature 362, 814-820). From the present immunochemical data, we further propose that locking the hinge movement with mAbs may induce lipase immunoinactivation.

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“…The co-lipase-PL complex can then bind to the bile salt covered interface thereby facilitating lipolysis. 58 As lipolysis progresses there is an accumulation of fatty acids and mono-glycerides at the emulsion interface that tend to desorb both gastric and pancreatic lipases from the interface. 59,60 Bile salts and phospholipids remove these digestion products from the interface by solubilizing them within mixed micelles dispersed in the aqueous phase, 55,61,62 thus promoting further lipid digestion.…”

Section: 22mentioning

confidence: 99%

The design of emulsions and their fate in the body following enteral and parenteral routes

Leal-Calderón

Cansell

2012

Soft Matter

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The approach of emulsified systems designed to enter the body is progressively shifting from empiricism to rational control. This paper reviews the literature related to the fate of oil-in-water emulsions in the body, more specifically in the gastrointestinal tract and in the blood stream. We address stability issues (coalescence and flocculation), interactions between droplets and endogenous biomolecules (chemicalbond cleaving enzymes, bio-surfactants, etc.) or organs, delivery of bioactive species and the most recent instrumentation advances. Overall, the review brings to light how colloidal oil droplets are processed in the body depending on their interfacial composition and their internal structure and/or composition.

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Studies on the detergent inhibition of pancreatic lipase activity.

Cited by 162 publications

References 26 publications

In vitro digestion of fish oils rich in n-3 polyunsaturated fatty acids studied in emulsion and at the oil–water interface

In vitro digestion of fish oils rich in n-3 polyunsaturated fatty acids studied in emulsion and at the oil–water interface

Human Pancreatic Lipase

The design of emulsions and their fate in the body following enteral and parenteral routes

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