IDEAS home Printed from https://ideas.repec.org/a/gam/jsusta/v15y2023i8p6618-d1123005.html
   My bibliography  Save this article

Thermodynamic Studies of the Micellar Properties of a Surfactant Used for Membrane Protein Solubilization and Stabilization

Author

Listed:
  • Joanna Krawczyk

    (Department of Interfacial Phenomena, Institute of Chemical Sciences, Faculty of Chemistry, Maria Curie-Skłodowska University in Lublin, Maria Curie-Skłodowska Sq. 3, 20-031 Lublin, Poland)

Abstract

The effect of temperature on the micellar properties of the alkylglucoside surfactant n -octyl- β -D-thioglucopyranoside (OTG) used for membrane protein solubilization has been investigated. Critical micelle concentration (CMC), apparent ( ϕ V ) and partial ( V ¯ M ) molar volume changes of the studied surfactant, as well as thermodynamic functions (the standard Gibbs free energy ( Δ G m i c o ), the standard enthalpy ( Δ H m i c o ) and entropy ( Δ S m i c o )) of the OTG micellization process were determined. The above-mentioned parameters were calculated on the basis of the results obtained from measurements of surface tension, density and viscosity of the aqueous solutions of n -octyl- β -D-thioglucopyranoside, as well as pyrene (Py) and 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescence intensity in aqueous solutions of OTG and dynamic light scattering of aqueous solutions of OTG. Basing on the obtained results it is stated that critical micelle concentration of OTG is much lower compared to that of the earlier studied n -octyl- β -D-glucopyranoside (OGP). The standard Gibbs free energy changes indicate that the tendency of OTG molecules to form aggregates increases with temperature increase. However, this increase is not so evident as in the case of some other sugar-based surfactants. The small temperature effect on the aggregation properties of OTG in water is probably connected with the presence and strength of the hydrogen bonds between the water molecules and sugar units, or the type of linkage between the hydrophobic and hydrophilic parts of the studied surfactant. In addition, the presence of S-linkage in the OTG molecule despite its high enzymatic stability also causes the hydrophobicity increase of the studied surfactant (compared to OGP), which directly influences its micellization process.

Suggested Citation

  • Joanna Krawczyk, 2023. "Thermodynamic Studies of the Micellar Properties of a Surfactant Used for Membrane Protein Solubilization and Stabilization," Sustainability, MDPI, vol. 15(8), pages 1-18, April.
  • Handle: RePEc:gam:jsusta:v:15:y:2023:i:8:p:6618-:d:1123005
    as

    Download full text from publisher

    File URL: https://www.mdpi.com/2071-1050/15/8/6618/pdf
    Download Restriction: no

    File URL: https://www.mdpi.com/2071-1050/15/8/6618/
    Download Restriction: no
    ---><---

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:gam:jsusta:v:15:y:2023:i:8:p:6618-:d:1123005. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: MDPI Indexing Manager (email available below). General contact details of provider: https://www.mdpi.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.