Microbial bio-production of a recombinant stimuli-responsive biosurfactant

Kaar, W., Hartmann, B. M., Fan, Y., Zeng, B., Lua, L. H. L., Dexter, A. F., Falconer, R. J. and Middelberg, A. P. J. (2009) Microbial bio-production of a recombinant stimuli-responsive biosurfactant. Biotechnology and bioengineering, 102 1: 176-187. doi:10.1002/bit.22037


Author Kaar, W.
Hartmann, B. M.
Fan, Y.
Zeng, B.
Lua, L. H. L.
Dexter, A. F.
Falconer, R. J.
Middelberg, A. P. J.
Title Microbial bio-production of a recombinant stimuli-responsive biosurfactant
Journal name Biotechnology and bioengineering   Check publisher's open access policy
ISSN 0006-3592
1097-0290
Publication date 2009-01-01
Sub-type Article (original research)
DOI 10.1002/bit.22037
Volume 102
Issue 1
Start page 176
End page 187
Total pages 12
Place of publication New York
Publisher Wiley Interscience
Language eng
Subject 100302 Bioprocessing, Bioproduction and Bioproducts
Abstract Biosurfactants have been the subject of recent interest as sustainable alternatives to petroleum-derived compounds in areas ranging from soil remediation to personal and health care. The production of naturally occurring biosurfactants depends on the presence of complex feed sources during microbial growth and requires multicomponent enzymes for synthesis within the cells. Conversely, designed peptide surfactants can be produced recombinantly in microbial systems, enabling the generation of improved variants by simple genetic manipulation. However, inefficient downstream processing is still an obstacle for the biological production of small peptides. We present the production of the peptide biosurfactant GAM1 in recombinant E. coli. Expression was performed in fusion to maltose binding protein using chemically defined minimal medium, followed by a single-step affinity capture and enzymatic cleavage using tobacco etch virus protease. Different approaches to the isolation of peptide after cleavage were investigated, with special emphasis on rapid and simple procedures. Solvent-, acid-, and heat-mediated precipitation of impurities were successfully applied as alternatives to post-cleavage chromatographic peptide purification, and gave peptide purities exceeding 90%. Acid precipitation was the method of choice, due to its simplicity and the high purification factor and recovery rate achieved here. The functionality of the bio-produced peptide was tested to ensure that the resulting peptide biosurfactant was both surface active and able to be triggered to switch between foam-stabilizing and foam-destabilizing states. Biotechnol. Bioeng. 2009;102: 176-187. © 2008 Wiley Periodicals, Inc.
Keyword Biosurfactant
Peptide
E. coli
Bio-production
Maltose binding protein
TEVp
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 12 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 13 times in Scopus Article | Citations
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Created: Fri, 15 May 2009, 13:57:38 EST by Ms Lynette Adams on behalf of Institute for Molecular Bioscience