Formation and structural heat-stability of β-lactoglobulin/surfactant complexes

Magdassi, Shlomo; Vinetsky, Yelena; Relkin, Perla

doi:10.1016/0927-7765(96)01266-0

Cited by 64 publications

(57 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Decreases in surface tension values of~-Ig in the presence of sodium dodecyl sulfate (SOS) or dodecyltrimethylammonium bromide (OTAB) have been previously observed [20]. In this last study, the surface tension values have been observed to reach a minimum for surfactant/~-Ig molar ratio close to 1, where formation of complexes between~-Ig and surfactant molecules have been shown.…”

Section: Spectrofluorimetric Measurementsmentioning

confidence: 50%

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

Marin¹,

Relkin²

1999

Lait

Self Cite

View full text Add to dashboard Cite

-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

show abstract

Section: Spectrofluorimetric Measurementsmentioning

confidence: 50%

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

Marin¹,

Relkin²

1999

Lait

Self Cite

View full text Add to dashboard Cite

show abstract

“…Thereby the repulsive force is reduced and this is why aggregation occurs. 35,36,38 The maximal diameter in BSA/12-n-12 aggregates is observed at c s ¼ 10 À4 M, in which the charges on BSA are almost completely neutralized, that is, the BSA/12-n-12 complex has a net charge close to zero. However, with further increasing 12-n-12 concentration (c s > 10 À4 M), while the average number of binding 12-n-12 increases rapidly, the hydrodynamic diameter decreases attributed to the dissociation of BSA/12-n-12 aggregates.…”

Section: Hydrodynamic Diametermentioning

confidence: 97%

“…With increasing surfactant concentration, a binding isotherm normally shows three characteristic regions prior to saturation as shown in Figure 3: (i) specific binding, (ii) noncooperative binding, and (iii) cooperative binding. 8,9,[31][32][33][34][35][36] In region (i) at c s < 2 Â 10 À5 M, the average number v of bound surfactant molecules rises marginally. In region (ii) between 2 Â 10 À5 M and 10 À4 M, slow but distinct increase in v is observed, in which the maximum of intrinsic fluorescence intensity decreases as seen in Figure 2.…”

Section: Intrinsic Fluorescencementioning

confidence: 99%

Interactions between bovine serum albumin and gemini surfactant alkanediyl‐α, ω‐bis(dimethyldodecyl‐ammonium bromide)

Shang

Peng

et al. 2006

Biopolymers

View full text Add to dashboard Cite

Interactions between bovine serum albumin (BSA) and cationic gemini surfactant alkanediyl-alpha,omega-bis(dimethyldodecyl-ammonium bromide) (12-n-12, n=3, 4, 6) in aqueous solution have been investigated by measuring fluorescence, UV-vis transmittance, dynamic lighting scattering, and circular dichroism. Compared to a traditional surfactant dodecyltrimethylammonium bromide (DTAB), 12-n-12 interacts with BSA more strongly. With increasing concentration, 12-n-12 first binds specifically onto BSA leading to the unfolding and aggregation of BSA, and the decrease in alpha-helix content; and then forms micelle-like complexes along the unfolded BSA chains. A gemini surfactant with a longer spacer has a larger effect on BSA unfolding due to a stronger hydrophobic interaction.

show abstract

“…At relatively higher protein concentration the formation of a viscous gel phase was identified. The interactions between anionic surfactants and proteins have been more extensively studied than those between protein and cationic surfactants (Kaneshina et al 1973;Nozaki et al 1974;Subramanian et al 1984;Subramanian et al 1986;Ericsson and Hegg, 1987;Prieto et al 1993;Magdassi et al 1996). It has been observed that cationic surfactants show a weaker primary interaction with proteins compared with anionic surfactants (Nozaki et al 1974;Ananthapadmanabhan, 1993).…”

Section: Effect Of Ionic and Non-ionic Additives In The Textile Bathsmentioning

confidence: 99%

Protein interactions in enzymatic processes in textiles

Tzanov¹,

Andreaus²,

Guebitz³

et al. 2003

Electron. J. Biotechnol.

View full text Add to dashboard Cite

Enzymes are the catalysts of all reactions in living systems. These reactions are catalysed in the active sites of globular proteins. The proteins are composed by amino acids with a variety of side chains ranging from non-polar aliphatic and aromatic to acidic, basic and neutral polar. This fact allows to a globular 3D protein to create in the active site all ranges of microenvironments for catalysis. Major advances in microbial technology and genetics allow recently the broad range of enzymatic applications in the industry. Enzymatic processes have been increasingly incorporated in textiles over the last years. Cotton, wool, flax or starches are natural materials used in textiles that can be processed with enzymes. Enzymes have been used for desizing, scouring, polishing, washing, degumming, peroxide degradation in bleaching baths as well as for decolourisation of dyehouse wastewaters, bleaching of released dyestuff and inhibiting dye transfer. Furthermore many new applications are under development such as natural and synthetic fibres modification, enzymatic dyeing, finishing etc. Most of the textile processes are heterogeneous where an auxiliary as a dye, enzyme, softener or oxidant have to *Corresponding author be taken from the solution to the fibre. These processes require the presence of surface-active agents, ionic force "balancers", buffers, stabilisers and others, and are characterized with high turbulence and mechanical agitation in the textile baths. In this paper it is intended to understand and discuss the major protein interactions within textile processes and to try to anticipate troubleshooting possibilities when enzymes are used. It can be expected that an enzyme protein can interact with all chemical agents in solution due to the large variety of side chains of the outer-amino-acids in the large 3D structure of the protein. Without the aim of being exhaustive various points will be discussed where protein interactions are important for textile processing.

show abstract

Formation and structural heat-stability of β-lactoglobulin/surfactant complexes

Cited by 64 publications

References 12 publications

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

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

Interactions between bovine serum albumin and gemini surfactant alkanediyl‐α, ω‐bis(dimethyldodecyl‐ammonium bromide)

Protein interactions in enzymatic processes in textiles

Contact Info

Product

Resources

About