A cryo-TEM study of protein-surfactant gels and solutions

Anna Karin Morén, Oren Regev, Ali Khan

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

Oppositely charged globular protein and surfactant systems, such as lysozyme-sodium dodecyl sulfate (SDS) and ovalbumindodecyltrimethylammonium chloride (DOTAC) form precipitate, gel, and colorless solution in water over a wide concentration range. Bluish solutions are also recognized in connection with the redissolution of precipitate as well as prior to the gel formation. For the lysozyme-SDS system the bluish solution has been suggested to consist of finely dispersed gel particles in solution. The oppositely charged bovine serum albumin (BSA)-DOTAC-water system forms only a large, clear solution phase and a narrow, bluish solution region within a very limited surfactant concentration range. In the lysozyme-SDS system the formation of protein-surfactant aggregates and their growth and breakdown are studied in detail by cryogenic-transmission electron microscopy (cryo-TEM) method. In particular a series of samples with an increased surfactant concentration at fixed 4 wt% of lysozyme is studied. Imaging of the bluish solution at different protein concentrations exhibits large aggregates in the form of rod-like, sheet-like, and star-like objects which are attributed to the gel. At excess amounts of SDS, in the colorless solution, only small objects are detected. In the ovalbumin-DOTAC-water and BSA-DOTAC-water systems large aggregates are also observed in the bluish solutions. Colorless solutions for these two systems show the presence of small objects in the cryo-TEM micrographs. Ultrathin sections of the lysozyme and ovalbumin gels fixed with OsO4 also show the presence of aggregated structures as judged from the transmission electron microscopy observations. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)170-178
Number of pages9
JournalJournal of Colloid and Interface Science
Volume222
Issue number2
DOIs
StatePublished - 15 Feb 2000

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