Interaction of Fatty Acids with β-Lactoglobulin and Albumin from Ruminant Milk1

Pérez, María Dolores; Villegas, Conchita Díaz de; Sánchez, Lourdes; Aranda, Paloma; Ena, J.M.; Calvo, Miguel

doi:10.1093/oxfordjournals.jbchem.a122971

Cited by 115 publications

(84 citation statements)

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“…The binding site in ␤-Lg is rather fully extended, but there is space for longer fatty acid molecules such as stearate and oleate to be accommodated within the calyx, with the carboxyl group making the same interactions with Lys-60 and Lys-69. The association constants for both acids are similar (33,34). In the fatty acid-binding protein family, palmitate is also observed in an extended form, although alternative conformations of bound fatty acids have been observed (35,36).…”

Section: Complex Of Palmitate With ␤-Lactoglobulinmentioning

confidence: 85%

β-Lactoglobulin Binds Palmitate within Its Central Cavity

Pérez

Puyol

et al. 1999

Journal of Biological Chemistry

310

304

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Section: Complex Of Palmitate With ␤-Lactoglobulinmentioning

confidence: 85%

β-Lactoglobulin Binds Palmitate within Its Central Cavity

Pérez

Puyol

et al. 1999

Journal of Biological Chemistry

310

304

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“…1 and references therein). ␤-Lactoglobulins isolated from cow, goat, and sheep milk samples, under nondenaturing conditions, showed endogenously bound fatty acids (2). Many authors have suggested that bovine ␤-lactoglobulin (BLG) 1 has a transport and/or protective role toward bound ligands in the stomach (3).…”

mentioning

confidence: 99%

EF Loop Conformational Change Triggers Ligand Binding in β-Lactoglobulins

Ragona

Fogolari

Catalano

et al. 2003

Journal of Biological Chemistry

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␤-Lactoglobulins, belonging to the lipocalin family, are a widely studied group of proteins, characterized by the ability to solubilize and transport hydrophobic ligands, especially fatty acids. Despite many reports, the mechanism of ligand binding and the functional role of these proteins is still unclear, and many contradicting concepts are often encountered in the literature. In the present paper the comparative analysis of the binding properties of ␤-lactoglobulins has been performed using sequence-derived information, structure-based electrostatic calculations, docking simulations, and NMR experiments. Our results reveal for the first time the mechanism of ␤-lactoglobulin ligand binding, which is completely determined by the opening-closing of EF loop, triggered by Glu 89 protonation. The alkaline shift observed for Glu 89 pK a in porcine ␤-lactoglobulin (pK a 9.7) with respect to the bovine species (pK a 5.5) depends upon the interplay of electrostatic effects of few nearby key residues. Porcine protein is therefore able to bind fatty acids provided that the appropriate pH solution conditions are met (pH > 8.6), where the EF loop conformational change can take place. The unusually high pH of binding detected for porcine ␤-lactoglobulin seems to be functional to lipases activity. Theoretical pK a calculations extended to representative ␤-lactoglobulins allowed the identification of key residues involved in structurally and functionally important electrostatic interactions. The results presented here provide a strong indication that the described conformational change is a common feature of all ␤-lactoglobulins.The physicochemical and biological characteristics of ␤-lactoglobulins, which belong to the lipocalin family, have been extensively studied in the last 30 years, but despite the wealth of data, the biological function of these extracellular proteins is still undefined (Ref. 1 and references therein). ␤-Lactoglobulins isolated from cow, goat, and sheep milk samples, under nondenaturing conditions, showed endogenously bound fatty acids (2). Many authors have suggested that bovine ␤-lactoglobulin (BLG) 1 has a transport and/or protective role toward bound ligands in the stomach (3). However, we have previously shown (4) that BLG, despite its high stability at acidic pH, is unable to bind fatty acids at low pH, thus indicating that it could not be employed "as is" as a transporter through the human gastric tract.Retinoids and fatty acids have been reported to bind to BLG in vitro in the pH range of 6.5-8.5, with dissociation constants on the order of 65 nM and 0.6 M, respectively (5). Specifically, titration experiments of BLG with palmitic acid (PA) (4) have clearly shown that: (i) at neutral pH the primary site for palmitic acid binding is within the protein calyx; (ii) the amount of bound PA is drastically reduced upon decreasing pH and the ligand is completely released at pH 2; (iii) in the pH range 7.3-6.4, a conformational equilibrium was observed for the bound ligand reflecting the dynamics of EF l...

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“…Therefore, either beneficial or detrimental changes can be produced as a result of high-pressure treatment [52]. 4.2 Effects of high hydrostatic pressure on functional properties of β-LG β-LG binds fatty acids in vivo [53] and a large variety of hydrophobic ligands in vitro [54], such as retinol, sodium dodecyl sulphate [55], and aroma compounds [56]. β-LG is known to interact with many flavor compounds, such as aldehydes, ketones [57], ionones [58], and hydrocarbons [59].…”

Section: Pressure-induced Changes In Protein Structurementioning

confidence: 99%

Changes in structure and functional properties of whey proteins induced by high hydrostatic pressure: A review

Liu

Jia

Clark

2009

Front. Chem. Eng. China

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High hydrostatic pressure (HHP) is an alternative technology to heat processing for food product modifications. It does not cause environmental pollution and eliminates the use of chemical additives in food products. This review covers the research conducted to understand the effect of HHP on structure and functional properties of whey proteins. In this paper, the mechanism underlying pressure-induced changes in β-lactoglobulin and α-lactabumin is also discussed and how they related to functional properties such as hydrophobicity, foam stability, and flavor-binding capacity.

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Interaction of Fatty Acids with β-Lactoglobulin and Albumin from Ruminant Milk1

Cited by 115 publications

References 0 publications

β-Lactoglobulin Binds Palmitate within Its Central Cavity

β-Lactoglobulin Binds Palmitate within Its Central Cavity

EF Loop Conformational Change Triggers Ligand Binding in β-Lactoglobulins

Changes in structure and functional properties of whey proteins induced by high hydrostatic pressure: A review

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