Effect of Oil Hydrophobicity on the Adsorption and Rheology of β-Lactoglobulin at Oil-Water Interfaces Jotam Bergfreund, Pascal Bertsch, Simon Kuster, and Peter Fischer.
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| Title: | Effect of Oil Hydrophobicity on the Adsorption and Rheology of β-Lactoglobulin at Oil-Water Interfaces Jotam Bergfreund, Pascal Bertsch, Simon Kuster, and Peter Fischer. |
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| Authors: | Bergfreund, Jotam1 jotam.bergfreund@hest.ethz.ch, Bertsch, Pascal1, Kuster, Simon1, Fischer, Peter1 peter.fischer@hest.ethz.ch |
| Source: | Langmuir. 4/24/2018, Vol. 34 Issue 16, p4929-4936. 8p. |
| Subjects: | Oil-water interfaces, Lactoglobulins, Globular proteins, Adsorption (Chemistry), Ionic strength, Denaturation of proteins |
| Abstract: | The adsorption of protein layers at oil-water interfaces is critical to the formation and stability of various emulsions in, for example, technical applications as well as in biological lipid storage. Effects of ionic strength, pH, temperature, and pretreatments of the proteins are well-known. However, the oil phase has been regarded as exchangeable and its role in protein adsorption has been widely ignored. Herein, the influence of systematically selected oil interfaces of high purity on the formation and properties of β-lactoglobulin (β-lg) adsorption layers was evaluated. Droplet profile tensiometry and interfacial rheometry were employed to determine the adsorption kinetics and dilatational and interfacial shear moduli. We show that depending on the molecular size, flexibility, hydrophobicity, polarity, and polarizability of the oils, globular proteins adsorb distinctively. Stronger interactions of polar oils with the hydrophilic exterior of the native β-lg lead to decelerated protein unfolding. This results in lower surface pressures and slower formation of viscoelastic networks. In addition, polar oils interact stronger with the protein network by hydrophilic bonding and thereby act as softening agents. The observed effects of hydrophobic subphases on the adsorbed protein layers provide knowledge, which promotes higher reproducibility in rheological studies and precise tailoring of interfacial films for enhanced formation and stability of emulsions. [ABSTRACT FROM AUTHOR] |
| Copyright of Langmuir is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
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| Items | – Name: Title Label: Title Group: Ti Data: Effect of Oil Hydrophobicity on the Adsorption and Rheology of β-Lactoglobulin at Oil-Water Interfaces Jotam Bergfreund, Pascal Bertsch, Simon Kuster, and Peter Fischer. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Bergfreund%2C+Jotam%22">Bergfreund, Jotam</searchLink><relatesTo>1</relatesTo><i> jotam.bergfreund@hest.ethz.ch</i><br /><searchLink fieldCode="AR" term="%22Bertsch%2C+Pascal%22">Bertsch, Pascal</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Kuster%2C+Simon%22">Kuster, Simon</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Fischer%2C+Peter%22">Fischer, Peter</searchLink><relatesTo>1</relatesTo><i> peter.fischer@hest.ethz.ch</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Langmuir%22">Langmuir</searchLink>. 4/24/2018, Vol. 34 Issue 16, p4929-4936. 8p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Oil-water+interfaces%22">Oil-water interfaces</searchLink><br /><searchLink fieldCode="DE" term="%22Lactoglobulins%22">Lactoglobulins</searchLink><br /><searchLink fieldCode="DE" term="%22Globular+proteins%22">Globular proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Adsorption+%28Chemistry%29%22">Adsorption (Chemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22Ionic+strength%22">Ionic strength</searchLink><br /><searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: The adsorption of protein layers at oil-water interfaces is critical to the formation and stability of various emulsions in, for example, technical applications as well as in biological lipid storage. Effects of ionic strength, pH, temperature, and pretreatments of the proteins are well-known. However, the oil phase has been regarded as exchangeable and its role in protein adsorption has been widely ignored. Herein, the influence of systematically selected oil interfaces of high purity on the formation and properties of β-lactoglobulin (β-lg) adsorption layers was evaluated. Droplet profile tensiometry and interfacial rheometry were employed to determine the adsorption kinetics and dilatational and interfacial shear moduli. We show that depending on the molecular size, flexibility, hydrophobicity, polarity, and polarizability of the oils, globular proteins adsorb distinctively. Stronger interactions of polar oils with the hydrophilic exterior of the native β-lg lead to decelerated protein unfolding. This results in lower surface pressures and slower formation of viscoelastic networks. In addition, polar oils interact stronger with the protein network by hydrophilic bonding and thereby act as softening agents. The observed effects of hydrophobic subphases on the adsorbed protein layers provide knowledge, which promotes higher reproducibility in rheological studies and precise tailoring of interfacial films for enhanced formation and stability of emulsions. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Langmuir is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1021/acs.langmuir.8b00458 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 8 StartPage: 4929 Subjects: – SubjectFull: Oil-water interfaces Type: general – SubjectFull: Lactoglobulins Type: general – SubjectFull: Globular proteins Type: general – SubjectFull: Adsorption (Chemistry) Type: general – SubjectFull: Ionic strength Type: general – SubjectFull: Denaturation of proteins Type: general Titles: – TitleFull: Effect of Oil Hydrophobicity on the Adsorption and Rheology of β-Lactoglobulin at Oil-Water Interfaces Jotam Bergfreund, Pascal Bertsch, Simon Kuster, and Peter Fischer. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Bergfreund, Jotam – PersonEntity: Name: NameFull: Bertsch, Pascal – PersonEntity: Name: NameFull: Kuster, Simon – PersonEntity: Name: NameFull: Fischer, Peter IsPartOfRelationships: – BibEntity: Dates: – D: 24 M: 04 Text: 4/24/2018 Type: published Y: 2018 Identifiers: – Type: issn-print Value: 07437463 Numbering: – Type: volume Value: 34 – Type: issue Value: 16 Titles: – TitleFull: Langmuir Type: main |
| ResultId | 1 |
