Batch Foam Fractionation of Kudzu (Pueraria lobata) Vine Retting Solution

  • Jirawat Eiamwat
  • Veara Loha
  • Aleš Prokop
  • Robert D. Tanner
Part of the Applied Biochemistry and Biotechnology book series (ABAB)


The aqueous protein solution from kudzu (Pueraria lobata) vine retting broth, without the addition of other surfactants, was foam-fractionated in a vertical tubular column with multiple sampling ports. Time-varying trajectories of the total protein levels were determined to describe the protein behavior at six positions along the 1-m column. The lowest two trajectories of this batch process represented a loss of proteins from the bulk liquid and tended to merge and decay together in time; the other trajectories displayed a gain in proteins in the foam phase. These upper column port protein concentration trajectories generally increased in time up to 45 min, followed by a decrease, reflecting the removal of proteins from the column ports. The foam became dryer as it passed up the column to the top port. The protein concentration was about 5–8 × higher in the top port foam than in the initial bulk solution, mainly as a result of liquid drainage from the foam along the column axis. This concentration increase in the collected foam was dependent on the initial pH of the bulk solution. The mol-wt profile of the proteins in the concentrated foam effluent was determined by one-dimensional gel electrophoresis. An analysis of the gel electropherograms indicated that the most abundant proteins could be cellulases and pectinases.


Apply Biochemistry Bulk Solution Total Protein Concentration Foam Fractionation Liquid Foamate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Schutz, F. (1937), Nature, 629, 630.Google Scholar
  2. 2.
    Bader, R. and Schutz, F. (1954), Nature, 183, 184.Google Scholar
  3. 3.
    Lalchev, Z., Dimitrova, L., Tzvetkova, P., and Exerowa, D. (1982), Biotechnol. Bioeng. 24, 2253–2262.CrossRefGoogle Scholar
  4. 4.
    Loha, V., Tanner, R. D., and Prokop, A. (1997), Appl. Biochem. Biotechnol. 63-65, 395–408.CrossRefGoogle Scholar
  5. 5.
    Lemlich, R. (1972), Adsorptive Bubble Separation Techniques, Academic, New York, pp. 1–50.CrossRefGoogle Scholar
  6. 6.
    Prokop, A., and Tanner, R. D. (1993), Starch/Stärke 45, 154.CrossRefGoogle Scholar
  7. 7.
    Uludag, S., Prokop, A., and Tanner, R. D. (1996), J. Sci. Ind. Res. 55, 381, 382.Google Scholar
  8. 8.
    Akkawi, J. S. (1990), US Patent, 4,891,096.Google Scholar
  9. 9.
    Bajpai, R. K., Prokop, A., and Tanner, R. D. (1993), Biotech. Adv. 11, 637.Google Scholar
  10. 10.
    Uludag, S., Loha, V., Prokop, A., and Tanner, R. D. (1996), Appl. Biochem. Biotechnol. 57/58, 76.CrossRefGoogle Scholar
  11. 22.
    Bradford, M. M. (1976), Anal. Biochem. 72, 248–254.CrossRefGoogle Scholar
  12. 12.
    Laemmli, U. K. (1970), Nature 227, 680–685.CrossRefGoogle Scholar
  13. 13.
    Reed, G. (1975), Enzymes in Food Processing, 2nd ed. Academic, New York, p. 102. 24. Leatham, G. F. and Himmel, M. E. (eds.) (1991), ACS Symposium Series 460, American Chemical Society, Washington, DC, p. 446.Google Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Jirawat Eiamwat
    • 1
  • Veara Loha
    • 1
  • Aleš Prokop
    • 1
  • Robert D. Tanner
    • 1
  1. 1.Department of Chemical EngineeringVanderbilt UniversityNashvilleUSA

Personalised recommendations