Effect of temperature on tryptophan fluorescence of β-lactoglobulin B

Mills, O. E.

doi:10.1016/0005-2795(76)90224-5

Cited by 79 publications

(44 citation statements)

References 13 publications

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“…Reddy et al 9 ) reported that an increase in the fluorescence intensity (F max) accompanied by a red shift in Amax at pH S and the quenching of the fluorescence intensity (Fmax) at pH 2 occurred in p-Iactoglobulin during heating in the solution. Our observation obtained in dry-heating of p-Iactoglobulin is consistent with that of the heating in a solution at pH S. Miles 10 ) reported that quenching of Fmax during heating of p-lactoglobulin in acidic solution is attributed to the conformational changes leading to the exposure of tryptophan groups to the polar enviroment. Therefore, the increase in F max during dry-heating can be explained on the structural and conformational basis as follows.…”

Section: Resultssupporting

confidence: 90%

Improvement of the Surface Functional Properties ofβ-Lactoglobulin andα-Lactalbumin by Heating in a Dry State

Ibrahim

Kobayashi

Kato

1993

Bioscience, Biotechnology, and Biochemistry

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Section: Resultssupporting

confidence: 90%

Improvement of the Surface Functional Properties ofβ-Lactoglobulin andα-Lactalbumin by Heating in a Dry State

Ibrahim

Kobayashi

Kato

1993

Bioscience, Biotechnology, and Biochemistry

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“…Under our experimental conditions, we observed no change in the wavelength of maximum fluorescence intensity for non-heated mixtures, relative to non-heated p-lg alone (figure 3a). As expected from earlier studies [24], tryptophan spectrofluorimetric spectra (figure 3b) showed that pre-heating the pure protein solution from 20 "C to 80 "C, led to increased value of maximum fluorescence intensity (+ 15 %) and to a Stokes' shift (3 to 4 nm), in compararison with unheated proteins, where the maximum wavelength of fluorescence intensity was observed at 333 nm. The increased value in maximum fluorescence intensity and the red-shift in its wavelength indicates more exposure of initially buried hydrophobie residues of p-lg molecules to the aqueous medium, after the heating/cooling.…”

Section: Spectrofluorimetric Propertiessupporting

confidence: 86%

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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“…According to the current interpretation of protein tryptophan fluorescence data (Permyakov et al, 1982(Permyakov et al, , 1985, and to previous intrinsic fluorescence studies on /~-LG (Mills, 1976), it appears that exposure of the protien at temperatures below 60~ resulted in a reversible modification of the hydrophobic regions around the protein tryptophans. The increase in ~,~m, should have resulted from increased exposure of the tryptophan residues to the solvent, and the decreased quantum yield to their interaction with quenching groups.…”

Section: Intrinsic Fluorescence Studies Showmentioning

confidence: 76%

Reversible and irreversible modifications ofβ-lactoglobulin upon exposure to heat

1994

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Modifications in the exposure to the solvent of hydrophobic residues, changes in their organization into surface hydrophobic patches, and alterations in the dimerization equilibrium of beta-lactoglobulin upon thermal treatment at neutral pH were studied. Exposure of tryptophan residues was temperature dependent and was essentially completed on the time scale of seconds. Reorganization of generic hydrophobic protein patches on the protein surface was monitored through binding of 1,8-anilinonaphthalenesulfonate, and was much slower than changes in tryptophan exposure. Different phases in surface hydrophobicity changes were related to the swelling and the subsequent collapse of the protein, which formed a metastable swollen intermediate. Heat treatment of beta-lactoglobulin also resulted in the formation of soluble oligomeric aggregates. The aggregation process was studied as a function of temperature, demonstrating that (i) dimer dissociation was a necessary step in a sequential polymerization mechanism and (ii) cohesion of hydrophobic patches was the major driving force for aggregation.

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Effect of temperature on tryptophan fluorescence of β-lactoglobulin B

Cited by 79 publications

References 13 publications

Improvement of the Surface Functional Properties ofβ-Lactoglobulin andα-Lactalbumin by Heating in a Dry State

Improvement of the Surface Functional Properties ofβ-Lactoglobulin andα-Lactalbumin by Heating in a Dry State

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

Reversible and irreversible modifications ofβ-lactoglobulin upon exposure to heat

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