β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acid uptake

Maux, Solène Le; Brodkorb, André; Croguennec, Thomas; Hennessy, Alan A.; Bouhallab, Saı̈d; Giblin, Linda

doi:10.3168/jds.2013-6682

Cited by 10 publications

(4 citation statements)

References 59 publications

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“…However, using a Caco-2 monolayer that mimics the intestinal barrier in combination with confocal imaging, the transport of linoleate into Caco-2 cells was decreased in the presence of β-lg in agreement with the cytotoxicity study (Le Maux et al 2013b). Retinol and palmitic acid were also transported more efficiently across the monolayer in its free form than in complex with β-lg (Puyol et al 1995; Riihimäki-Lampén 2009).…”

Section: Biological Properties Of the β-Lactoglobulin/ligand Complexessupporting

confidence: 85%

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties

Maux

Bouhallab

Giblin

et al. 2014

Dairy Sci. & Technol.

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121

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Ligand-binding properties of β-lactoglobulin (β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an interest in the binding properties of native β-lg (localization of binding sites, stoichiometry, and affinity) and the way the interaction affects the biological properties of the protein and the ligand. The binding properties of non-native aggregated forms of β-lg that are classically generated during industrial processing are also related. Structural changes modify the stoichiometry and the affinity of β-lg for fatty acids and consequently the biological functions of the complex. Finally, the fatty acid-binding properties of other whey proteins (α-lactalbumin, bovine serum albumin) and some biological properties of the complexes are also addressed. These proteins affect β-lg/fatty acids complex in whey given their competition with β-lg for fatty acids.

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Section: Biological Properties Of the β-Lactoglobulin/ligand Complexessupporting

confidence: 85%

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties

Maux

Bouhallab

Giblin

et al. 2014

Dairy Sci. & Technol.

Self Cite

121

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“…However, the dissociation is reversible so that the reformation of the complex upon increase in the pH value can occur. 153 Furthermore, it has been postulated that small hydrophobic molecules inside the calyx may be protected from the environment by a closed EF-loop. 150 Thus, complexation is affected by the size and chemical structure of the BC.…”

Section: Protein Based Enmmentioning

confidence: 99%

“…157 Despite the high pH value in the intestinal lumen, a release of substances located in the calyx can occur near cell surfaces where a lower pH is present and therefore dissociation of the complex is favoured. 153 Caseins have a large number of proline residues, a high net charge and low intrinsic hydrophobicity leading to a unique unfolded structure under native conditions. In milk, caseins are usually present in the form of micelles which are formed by hydrophobic interactions and colloidal calcium phosphate bridges and are 50-500 nm in diameter.…”

Section: Protein Based Enmmentioning

confidence: 99%

Potential bioavailability enhancement of bioactive compounds using food-grade engineered nanomaterials: a review of the existing evidence

et al. 2014

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The development of engineered nanometre sized materials (ENM) produced with food-grade ingredients and designed as delivery systems for organic and inorganic materials has gained increasing interest. The major reason for this trend is the aim to overcome problems associated with the low bioavailability of many bioactive compounds (BC) which are usually claimed to benefit human health. In this review, outcomes of studies investigating the potential bioavailability enhancement of BC using ENM as delivery systems are summarised and discussed. It focuses on in vitro and in vivo studies carried out with ENM produced with food-grade materials and designed for the delivery of vitamins, other secondary plant metabolites and minerals. Furthermore, the physical and physicochemical aspects governing the preparation of the systems, the loading of the BC, the stability of the delivery systems in food applications and finally the release of the BC in the gastrointestinal tract are also considered. The mechanisms leading to an enhanced bioavailability are based on (i) improved solubility of the BC under gastrointestinal conditions, (ii) the protection of the BC from the chemical conditions in the gastrointestinal tract (GIT), (iii) the controlled release within the GIT or (iv) an improved transfer through the intestinal wall. The main outcome of the review is that particle size, surface properties and physical state of the ENM are key parameters to be controlled aiming at an enhanced nutritional value of food materials. Furthermore, the bioavailability classification scheme (BCS) can help to understand the efficacy of different ENM for the delivery of specific BC.

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“…Moreover, they demonstrated that 12 % of riboflavin recommended daily dose reached the intestine if 100 mL of a food simulant solution was ingested. Le Maux, Brodkorb, Croguennec, and Hennessy (2013) investigated the potential changes in β-Lg/linoleate complex after static in vitro digestion, as well as the linoleate acid bioaccessibility and their intracellular transport into Caco-2 cells. These authors demonstrated that binding β-Lg to linoleic acid influences the protein susceptibility to digestion.…”

Section: Introductionmentioning

confidence: 99%

β-lactoglobulin micro- and nanostructures as bioactive compounds vehicle: In vitro studies

Simões

Martins

Pinheiro

et al. 2020

Food Research International

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Lactoglobulin (β-Lg) is known to be capable to bind hydrophilic and hydrophobic bioactive compounds. This research aimed to assess the in vitro performance of β-Lg micro-(diameter ranging from 200 to 300 nm) and nano (diameter < 100 nm) structures associated to hydrophilic and hydrophobic model compounds on Caco-2 cells and under simulated gastrointestinal (GI) conditions. Riboflavin and quercetin were studied as hydrophilic and hydrophobic model compounds, respectively. Cytotoxicity experiment was conducted using in vitro cellular model based on human colon carcinoma Caco-2 cells. Moreover, the digestion process was simulated using the harmonized INFOGEST in vitro digestion model, where samples were taken at each phase of digestion processoral, gastric and intestinal-and characterized in terms of particle size, polydispersity index (PDI), surface charge by dynamic light scattering (DLS); protein hydrolysis degree by 2,4,6-trinitrobenzene sulfonic acid (TNBSA) assay and native polyacrylamide gel electrophoresis; and bioactive compound concentration. Caco-2 cell viability was not affected up to 21 × 10 −3 mg mL −1 of riboflavin and 16 × 10 −3 mg mL −1 quercetin on β-Lg micro-and nanostructures. In the oral phase, β-Lg structures' particle size, PDI and surface charge values were not changed comparing to the initial β-Lg structures (i.e., before being subjected to in vitro GI digestion). During gastric digestion, β-Lg structures were resistant to proteolytic enzymes and to acid environment of the stomachconfirmed by TNBSA and native gel electrophoresis. In vitro digestion results indicated that β-Lg micro-and nanostructures protected both hydrophilic and hydrophobic compounds from gastric conditions and deliver them to target site (i.e., intestinal phase). In addition, β-Lg structures were capable to enhance riboflavin and quercetin bioaccessibility and bioavailability potential compared to bioactive compounds in their free form. This study indicated that β-Lg micro-and nanostructures were capable to enhance hydrophilic and hydrophobic compounds bioavailability potential and they can be used as oral delivery systems.

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β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acid uptake

Cited by 10 publications

References 59 publications

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties

Potential bioavailability enhancement of bioactive compounds using food-grade engineered nanomaterials: a review of the existing evidence

β-lactoglobulin micro- and nanostructures as bioactive compounds vehicle: In vitro studies

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