The relationship between hydrophobicity and interfacial tension of proteins

Keshavarz, Elaheh; Nakai, S.

doi:10.1016/0005-2795(79)90402-1

Cited by 116 publications

(48 citation statements)

References 15 publications

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“…This behaviour is similar to that of OVA on the surface of cationic surfactant-treated silica glass (which has a contact angle of about 75 º) observed in our previous study [Kawasaki et al, 1998]. Keshavarz and Nakai [1979] reported on the hydrophobicity of OVA, α-lactoalbumin, conalbumin, α-chymotrypsin, myoglobin, LAG, γ-globulin, LSZ and bovine serum albumin (BSA) surfaces based on hydrophobic affinity chromatography. They reported that the surface of OVA is more hydrophilic than those of the other proteins.…”

Section: Discussionsupporting

confidence: 88%

Measurements of the Wettability of Protein–Covered Hydroxyapatite Surfaces

1999

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We developed a new method (dropping time method, DTM) to investigate the wettability of a surface of a protein layer adsorbed on glass plates in aqueous solution. However, the previous setup of DTM can only be utilized for optically transparent materials. In this study, we have extended the method to optically nontransparent materials such as hydroxyapatite plates. DTM is based on measuring the dropping time of a liquid film along a protein–covered surface when this surface is instantaneously vertically removed from the protein solution. The intensity of the reflected light beam depends on the presence of a liquid film on the surface. This allows to estimate the movement of the liquid film along the sorbent surface. Thus, the extended DTM can be used for determining the wettability of optically nontransparent solid plates. The adsorption behavior of four proteins (albumin, lysozyme, β–lactoglobulin, ovalbumin) on a hydrophobic hydroxyapatite plate in water was studied by this method. When adsorbed from a protein solution of high concentration, the surfaces of adsorbed proteins, except ovalbumin, were fairly hydrophilic; this hydrophilicity was already attained at the initial stage of the adsorption process. The surface of ovalbumin on hydroxyapatite was more hydrophobic than those of the other proteins, and the hydrophilicity increased with the protein adsorption process. At low protein concentration, the hydrophilicity increased in the course of the adsorption process. The change in hydrophilicity with time depends on the kind of protein. Hen’s egg lysozyme is more hydrophilic and the time to reach saturation is shorter than for the other proteins. The processes of increasing hydrophilicity of the surface of human serum albumin, β–lactoglobulin and ovalbumin are similar. However, for β–lactoglobulin hydrophobicity at adsorption saturation is stronger than for human serum albumin and ovalbumin. Thus, using DTM it is shown that the hydrophilicity of the surface of adsorbed protein on hydroxyapatite depends strongly on the kind of protein.

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Section: Discussionsupporting

confidence: 88%

Measurements of the Wettability of Protein–Covered Hydroxyapatite Surfaces

1999

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“…The surface hydrophobicities of proteins at native state might be, therefore, not meaningful to evaluate their adsorbabilities at the interfaces, although Nakai et al have reported that the effective hydrophobicities (actual surface hydrophobicities) of proteins were significantly correlated with interfacial tensions 19 ) and emulsifying activities. 18 ) The easiness in changing the conformation of the protein molecules during the emulsification, in other words, the compactness or flexibility of proteins, would be a more important factor.…”

Section: Proteolytic Digestion Of Whey Proteins Adsorbed On the Fat Gmentioning

confidence: 99%

The Adsorption of Whey Proteins on the Surface of Emulsified Fat

Shimizu

Kamiya

Yamauchi

1981

Agricultural and Biological Chemistry

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“…Klein and Dhurjati (1995) studied CheY protein aggregation kinetics in Escherichia Coli and showed that proteins (polymers of α-amino acids) are able to aggregate in soluble and insoluble forms, and that the aggregation was time dependent. In addition, many studies showed that proteins could be adsorbed at interfaces and reduce the interfacial tension (Beverung et al, 1999;van der Vegt et al, 1996;Keshavarz et al, 1979). Furthermore, He et al (1998) showed that bacteria under certain growth condition are able to produce polymer compounds.…”

Section: Discussionmentioning

confidence: 99%