Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution

Monaco, Hugo L.; Zanotti, Giuseppe; Spadon, Paola; Bolognesi, Martino; Sawyer, Lindsay; Eliopoulos, Elias

doi:10.1016/0022-2836(87)90476-1

Cited by 336 publications

(250 citation statements)

References 42 publications

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“…This may be explained by a stabilization of the 4-vinylguaiacol-BLG-complex resulting from a structural analogy between the planar flavour compound and the planar side-chain of an amino acid in the hydrophobic pocket of BLG. Monaco et al [12] suggested that the planar ring of β-ionone was fixed by in comparison to the cis isomers. However, we observed no stereoselectivity of BLG for these compounds, which confirms the results obtained by Massolini et al [11].…”

Section: Affinity Chromatographymentioning

confidence: 99%

“…A possible binding site for retinol was identified by model-building. Monaco et al [12], who analyzed the structure of BLG using X-ray diffraction methods, located the binding site for retinol in a hydrophobic pocket on the surface of BLG. More recently, Wu et al [27] demonstrated, after co-crystallization of the complex, that palmitate was bound in the central cavity of the protein.…”

Section: Introductionmentioning

confidence: 99%

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Interactions between ?-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol

Reiners

Nicklaus

Guichard

2000

Lait

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-Interactions between β-lactoglobulin and flavour compounds were analysed by instrumental and sensory studies. Affinity chromatography was used to determine binding constants of flavour substances belonging to different chemical classes. A systematic study on esters, pyrazines and phenolic compounds revealed that the increase in the hydrophobic chain length increases the affinity for the protein. Concerning the 4 diastereoisomers of 3-oxo-p-menthane-8-thiol, only the cistrans isomery led to different binding constants. In general, binding constants increased with increasing log P values, except for the terpenic compounds studied, for which another explanation has to be found, taking into account the geometry of the molecule. Sensory analyses applying a matching test showed that the addition of β-lactoglobulin had no effect on the odour perception of vanillin, but brought about a significant decrease in the odour perception of eugenol.

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Section: Affinity Chromatographymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Interactions between ?-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol

Reiners

Nicklaus

Guichard

2000

Lait

View full text Add to dashboard Cite

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“…L'écart type de ces mesures est faible, toujours inférieur à ± 0,01 mg/1. (Eigel et al, 1984); -l'hydrophobicité : le variant A est un peu plus hydrophobe que le variant B (Cheftel et al, 1985); cependant, l'exposition à la surface de la molécule du variant A du ré-sidu aspartyl 64 (Monaco et al, 1987) Lorsqu'on étudie la prolifération cellulaire, on constate que les milieux supplé-mentés avec 2,7 g/I de B-Lg variant AlB et 1% de SVF sont aussi efficaces que les milieux supplémentés avec 9% de lactosé-rum. Donc, l'activité mitogénique du lactosérum semble être liée, au moins pour la plus grande partie, à la présence de la 13-Lg.…”

Section: Discussionunclassified

Rôle de la β-lactoglobuline dans l'activité proliférative du lactosérum

Moulti-Mati¹,

Mati²,

Capiaumont³

et al. 1991

Lait

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“…From its core-structural pattern, as revealed by X-ray crystallography [25,28], it has been suggested that hydrophobie ligands may bind inside the central calyx, and fromrecent studies [4,32,40], there is evidence that it binds fatty acids inside the centrai calyx, as for retinol.…”

Section: Introductionmentioning

confidence: 99%

Adsorption kinetics of β-lactoglobulin at the air / solution interface: impact of pre-heating and addition of isoamyl acetate

Marin¹,

Relkin²

1999

Lait

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-We compared the kinetics of adsorption at the air/solution interface of~-lactoglobulin alone or in mixture with isoamyl acetate at a concentration where it remains water-soluble. Addition of isoamyl acetate to~-Iactoglobulin, at molar ratios equal to 1 or 2, led to a decrease in the surface tension in the short-time region, but the steady-state value of surface tension was close to that of pre-heated solution of~-lactoglobulin alone, only for molar ratio equal to 2. Pre-heating mixtures at this molar ratio increased the adsorption kinetics more significantly in comparison with non-heated mixtures and pre-heated pure solutions of~-lactoglobuline. ln parallel, tryptophan spectrotluorimetric spectra obtained from non-heated or pre-heated solutions indicated in both cases that addition of isoamyl acetate to~-Iactoglobulin were accompanied by a quenching of fluorescence intensity, while a slight red-shift in wavelength of maximum tluorescence intensity occured only for pre-heated mixtures. The results were discussed in terms of formation of~-lg/lAA complexes with a specifie activity at the air/solution interface. © InralElsevier, Paris.-lactogIobulin / aroma compound / protein-ligand complex / surface activity / air-water interface 1. Marin, P. Relkin à 2. La cinétique d'adsorption à l'interface air/liquide, de la~-Iactoglobuline est nettement accélérée lorsque le mélange au rapport molaire égal à 2 a été préchauffé. Parallèlement, les spectres de fluorescence du tryptophane, obtenus à partir des différentes solutions étudiées, ont montré une diminution de l'intensité de fluorescence pour tous les mélanges~-Ig/AIA, alors qu'un léger déplacement vers le rouge de la longueur d'onde d'intensité maximale n'a été observé que dans le cas des mélanges pré-chauffés. Les différences de cinétique d'adsorption de la~-Iactoglobuline, observées dans les diffé-rentes conditions étudiées, sont discutées en termes de formation de complexe entre la~-Ig et le composé d'arôme, pouvant avoir une activité de surface spécifique. © InralElsevier, Paris.-Iactoglobuline / composé d'arôme / complexe protéine-ligand / activité de surface / interface eau-air

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Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution

Cited by 336 publications

References 42 publications

Interactions between ?-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol

Interactions between ?-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol

Rôle de la β-lactoglobuline dans l'activité proliférative du lactosérum

Adsorption kinetics of β-lactoglobulin at the air / solution interface: impact of pre-heating and addition of isoamyl acetate

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