Protein Concentration Dependence of Palmitate Binding to β-Lactoglobulin

Wang, Qiwu; Allen, Jonathan C.; Swaisgood, Harold E.

doi:10.3168/jds.s0022-0302(98)75553-5

Cited by 53 publications

(46 citation statements)

References 22 publications

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“…It was also found that fatty acids binding to lactoglobulin is significantly affected by protein concentration. Increase of protein concentration from 1 to 200 mM resulted in sixfold decrease of the association constant for primary palmitic acid binding site (Wang et al, 1998). Authors attributed this behaviour to existence of two independent binding sites, one in monomer and second in lactoglobulin dimer.…”

Section: Introductionmentioning

confidence: 94%

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Two modes of fatty acid binding to bovine β‐lactoglobulin—crystallographic and spectroscopic studies

Loch¹,

Polit²,

Górecki³

et al. 2010

J of Molecular Recognition

107

104

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Lactoglobulin is a natural protein present in bovine milk and common component of human diet, known for binding with high affinity wide range of hydrophobic compounds, among them fatty acids 12-20 carbon atoms long. Shorter fatty acids were reported as not binding to β-lactoglobulin. We used X-ray crystallography and fluorescence spectroscopy to show that lactoglobulin binds also 8- and 10-carbon caprylic and capric acids, however with lower affinity. The determined apparent association constant for lactoglobulin complex with caprylic acid is 10.8 ± 1.7 × 10(3) M(-1), while for capric acid is 6.0 ± 0.5 × 10(3) M(-1). In crystal structures determined with resolution 1.9 Å the caprylic acid is bound in upper part of central calyx near polar residues located at CD loop, while the capric acid is buried deeper in the calyx bottom and does not interact with polar residues at CD loop. In both structures, water molecule hydrogen-bonded to carboxyl group of fatty acid is observed. Different location of ligands in the binding site indicates that competition between polar and hydrophobic interactions is an important factor determining position of the ligand in β-barrel.

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Section: Introductionmentioning

confidence: 94%

“…These values indicate much weaker lactoglobulin affinity for caprylic and capric acid than for longer fatty acids. Apparent association constant reported by (Frapin et al, 1993;Wang et al, 1998). Later papers showed on the base of crystal structures that this primary binding site was located in central calyx Wu et al, 1999).…”

mentioning

confidence: 99%

Two modes of fatty acid binding to bovine β‐lactoglobulin—crystallographic and spectroscopic studies

Loch¹,

Polit²,

Górecki³

et al. 2010

J of Molecular Recognition

107

104

View full text Add to dashboard Cite

show abstract

“…It has been suggested that βlg binds hydrophobic ligands in its internal calyx, in a crevice near the α-helix on the external surface of the β-barrel and near the interface of βlg dimers (Lange et al, 1998, Wang et al, 1998, Wu et al, 1999, Muresan et al, 2001, Kontopidis et al, 2004, Forrest et al, 2005, Dong et al, 2006, Yang et al, 2008. However, the binding sites and stoichiometries of ligands have been controversial (Wang et al, 1998, Wu et al, 1999, Kontopidis et al, 2002. βlg may modify the transport, through the gastric tract of hydrophobic substances naturally present in bovine milk Calvo, 1995, Ragona et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

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

Maux¹,

Brodkorb²,

Croguennec³

et al. 2013

Journal of Dairy Science

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The dairy protein β-lactoglobulin (BLG) is known to bind fatty acids such as the salt of the essential longchain fatty acid linoleic acid (cis,cis-9,12-octadecadienoic acid, n-6, 18:2). The aim of the current study was to investigate how bovine BLG-linoleate complexes, of various stoichiometry, affect the enzymatic digestion of BLG and the intracellular transport of linoleate into enterocyte-like monolayers. Duodenal and gastric digestions of the complexes indicated that BLG was hydrolyzed more rapidly when complexed with linoleate. Digested as well as undigested BLG-linoleate complexes reduced intracellular linoleate transport as compared with free linoleate. To investigate whether enteroendocrine cells perceive linoleate differently when part of a complex, the ability of linoleate to increase production or secretion of the enteroendocrine satiety hormone, cholecystokinin, was measured. Cholecystokinin mRNA levels were different when linoleate was presented to the cells alone or as part of a protein complex. In conclusion, understanding interactions between linoleate and BLG could help to formulate foods with targeted fatty acid bioaccessibility and, therefore, aid in the development of food matrices with optimal bioactive efficacy

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“…Three independent tests were carried out in each case and SD was lower than 3.5 %. Inset: The emission spectrum of un-treated β-Lg (grey) and β-Lg-LA complex (black) (Frapin et al 1993;Wang et al 1998Wang et al , 1999. These studies also report that the β-Lg fluorescence intensity increased when fatty acids bound to the superficial pocket.…”

Section: Intrinsic Fluorescencementioning

confidence: 68%

“…2b) , who quenched its fluorescence. Two lipophilic ligand binding sites have been reported for β-Lg: a central hydrophobic β-barrel and a superficial pocket (Wang et al 1998(Wang et al , 1999. It seems that fatty acids bind at the superficial pocket, while other molecules bind to the calyx Fig.…”

Section: Intrinsic Fluorescencementioning

confidence: 99%

Exploring the heat-induced structural changes of β-lactoglobulin -linoleic acid complex by fluorescence spectroscopy and molecular modeling techniques

et al. 2015

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Linoleic acid (LA) is the precursor of bioactive oxidized linoleic acid metabolites and arachidonic acid, therefore is essential for human growth and plays an important role in good health in general. Because of the low water solubility and sensitivity to oxidation, new ways of LA delivery without compromising the sensory attributes of the enriched products are to be identified. The major whey protein, β-lactoglobulin (β-Lg), is a natural carrier for hydrophobic molecules. The thermal induced changes of the β-Lg-LA complex were investigated in the temperature range from 25 to 85°C using fluorescence spectroscopy techniques in combination with molecular modeling study and the results were compared with those obtained for β-Lg. Experimental results indicated that, regardless of LA binding, the polypeptide chain rearrangements at temperatures higher than 75°C lead to higher exposure of hydrophobic residues causing the increase of fluorescence intensity. Phase diagram indicated an all or none transition between two conformations. The LA surface involved in the interaction with β-Lg was about 497 Ǻ 2 , indicating a good affinity between those two components even at high temperatures. Results obtained in this study provide important details about heat-induced changes in the conformation of β-Lg-LA complex. The thermal treatment at high temperature does not affect the LA binding and carrier functions of β-Lg.

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Protein Concentration Dependence of Palmitate Binding to β-Lactoglobulin

Cited by 53 publications

References 22 publications

Two modes of fatty acid binding to bovine β‐lactoglobulin—crystallographic and spectroscopic studies

Two modes of fatty acid binding to bovine β‐lactoglobulin—crystallographic and spectroscopic studies

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

Exploring the heat-induced structural changes of β-lactoglobulin -linoleic acid complex by fluorescence spectroscopy and molecular modeling techniques

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