Peptides as functional surfactants

Dexter, Annette F. and Middelberg, Anton P. J. (2008) Peptides as functional surfactants. Industrial & Engineering Chemistry Research, 47 17: 6391-6398. doi:10.1021/ie800127f


Author Dexter, Annette F.
Middelberg, Anton P. J.
Title Peptides as functional surfactants
Journal name Industrial & Engineering Chemistry Research   Check publisher's open access policy
ISSN 0888-5885
Publication date 2008-09-03
Year available 2008
Sub-type Article (original research)
DOI 10.1021/ie800127f
Open Access Status
Volume 47
Issue 17
Start page 6391
End page 6398
Total pages 8
Editor D. R. Paul
S. D. Alexandratos
Place of publication Washington, D.C. U.S.A.
Publisher American Chemical Society
Language eng
Subject C1
100799 Nanotechnology not elsewhere classified
100302 Bioprocessing, Bioproduction and Bioproducts
860899 Human Pharmaceutical Products not elsewhere classified
Abstract Peptides offer interesting alternatives to conventional surfactants in applications where renewability, biocompatibility, or added functionality may be desired. This review offers a brief overview of different classes of surface-active peptides and lipopeptides, covering molecules obtained from natural sources as well as those obtained by design. Bacterial lipopeptides are cyclic molecules containing a single fatty acyl moiety, which can exhibit ultralow interfacial tension as well as antimicrobial activities. Bacterial lipopeptides have been proposed for industrial applications such as bioremediation and oil recovery, but they suffer the dual disadvantages of being difficult to bioproduce at low cost and not being easily genetically engineered. A class of synthetic molecules related to bacterial lipopeptides are the peptide amphiphiles, in which a peptide headgroup is combined with a peptide or nonpeptide hydrophobic tail. Self-assembly of peptide amphiphiles has largely been studied in bulk solution rather than at interfaces, meaning that very little information is available on the interfacial properties of these designer molecules. A larger body of information is available for protein hydrolysates, products of the partial breakdown of low-cost proteins (usually food proteins) into a complex mixture of small peptides. Partial hydrolysis can improve the functional properties of many proteins, but the outcomes are difficult to predict or control, and useful functional properties may be associated with only a few minor components in the digest mix. Finally, designed peptide surfactants (Pepfactants), recently reported by the authors, are facially amphipathic molecules that self-assemble at fluid interfaces to give cohesive films stabilizing foams and emulsions. A change in the bulk solution conditions can switch off the interfacial film, leading to rapid foam or emulsion collapse. Pepfactants can be genetically engineered and bioproduced using standard methods, which represents an advantage over bacterial lipopeptides. While peptides have not been widely used in surfactant applications so far, recent developments may facilitate the incorporation of these interesting molecules into industrial and consumer products in the near future.
Keyword Recombinant Bacillus-Subtilis
Interfacial Protein Networks
Solid-State Fermentation
Helical Coiled Coils
Emulsifying Properties
Microbial Surfactants
Mechanical-Properties
Beta-Lactoglobulin
Lipopeptide Biosurfactants
Potential Applications
Q-Index Code C1
Q-Index Status Confirmed Code

 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 50 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 56 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Fri, 17 Apr 2009, 00:48:20 EST by Amanda Lee on behalf of School of Chemical Engineering