β-Lactoglobulin heat-induced aggregates as carriers of polyunsaturated fatty acids

Pérez, Adrián A.; Andermatten, Romina Belén; Rubiolo, Amelia Catalina; Santiago, Liliana G.

doi:10.1016/j.foodchem.2014.02.073

Cited by 67 publications

(39 citation statements)

References 39 publications

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“…BLG aggregates would be more hydrophobic than native BLG because heat treatment could promote a greater exposition of buried hydrophobic domains. These changes in protein tertiary structure could be irreversible (Pérez et al 2014a).…”

Section: Modified Proteins As Nanocarriers Of Bioactive Compoundsmentioning

confidence: 99%

“…The assumption that heat-induced BLG aggregates with improved hydrophobic properties could have a greater ability to bind linolenic acid (LA) than native BLG was reported (Pérez et al 2014a). They also studied the effect of pH and concluded that BLG aggregates formed at pH 6.5 were the most hydrophobic.…”

Section: Modified Proteins As Nanocarriers Of Bioactive Compoundsmentioning

confidence: 99%

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Emerging Technologies for Bioactive Applications in Foods

2017

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Section: Modified Proteins As Nanocarriers Of Bioactive Compoundsmentioning

confidence: 99%

Section: Modified Proteins As Nanocarriers Of Bioactive Compoundsmentioning

confidence: 99%

Emerging Technologies for Bioactive Applications in Foods

2017

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“…Current researches in nutraceutical delivery strategies are bringing into attention the binding properties of β-lactoglobulin (β-Lg) (Livney 2010;Perez et al 2014;Sponton et al 2014). β-Lg is the major protein in whey and exists as a dimer with each monomer containing 162 aminoacid residues and a molecular mass of 18 kDa.…”

Section: Introductionmentioning

confidence: 99%

“…The monomer is a globular protein folded into a calyx called β-barrel that contains eight anti-parallel β-strands (A-H). As member of lipocalin family, it has the ability to bind and transport lipophilic nutrients such as retinol, fatty acids and vitamin D (Sahihi et al 2011;Mensi et al 2013;Keppler et al 2014;Perez et al 2014). The internal cavity does not possess direct access to the external aqueous environment, so that some sort of protein rearrangement is thought to occur during ligand binding and release.…”

Section: Introductionmentioning

confidence: 99%

“…However, β-Lg functional properties are easily modified by different processes that include: thermal treatment, high pressure, pH values etc. (Sahihi et al 2011;Liang and Subirade 2012;Perez et al 2014). As a consequence, the binding properties are influenced not only by the ligand physicochemical properties but also by the protein structural transitions.…”

Section: Introductionmentioning

confidence: 99%

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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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