Skip to main content
Log in

Effects of surfactants, pH, and certain cations on precipitation of proteins by tannins

  • Published:
Journal of Chemical Ecology Aims and scope Submit manuscript

Abstract

Tannic acid and pin oak tannins precipitate large amounts of the abundant leaf protein, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBPC), over a wide pH range (6.15–9.30) in the presence of sodium, potassium, magnesium, and calcium ions at concentrations comparable to those reported in the gut fluids of lepidopteran herbivores. The presence of lysolecithin, a surfactant known to be present in the gut fluids of some insects, significantly reduces the amount of RuBPC precipitated under these conditions. We conclude that high detergency is far more effective than high alkalinity in countering the potential protein-precipitating properties of tannins. We further conclude that tannins do not deserve the status they were once accorded as general, all-purpose, dose-dependent, antidigestive defensive chemicals. We also describe the application of the Schaffner-Weissman protein assay for studying the protein-precipitating capacity of plant extracts. This method is far superior to the one we have used in our earlier studies.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Akazawa, T. 1970. The structure and function of fraction-I protein.Prog. Phytochem. 2:107–141.

    Google Scholar 

  • Berenbaum, M. 1980. Adaptive significance of midgut pH in larval Lepidoptera.Am. Nat. 115:138–146.

    Google Scholar 

  • Bernays, E.A. 1981. Plant tannins and insect herbivores: An appraisal.Ecol. Entomol. 6:353–360.

    Google Scholar 

  • Bradford, M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein—dye-binding.Anal. Biochem. 72:248–254.

    PubMed  Google Scholar 

  • Feeny, P.P. 1970. Seasonal changes in oak leaf tannins and nutrients as a cause of spring feeding by winter moth caterpillars.Ecology 51:565–581.

    Google Scholar 

  • Feeny, P. 1976. Plant apparency and chemical defense.Recent Adv. Phytochem. 10:1–40.

    Google Scholar 

  • Giordana, B., andSacchi, F. 1978. Cellular ionic concentrations in the midgut of two larvae of Lepidoptera in vivo and in vitro.Comp. Biochem. Physiol. 59A:17–20.

    Google Scholar 

  • Goldstein, J.L., andSwain, T. 1965. The inhibition of enzymes by tannins.Phytochemistry 4:185–192.

    Google Scholar 

  • Hagerman, A., andButler, L. 1978. Protein precipitation method for the quantitative determination of tannins.J. Agric. Food Chem. 26:809–812.

    Google Scholar 

  • Hagerman, A.E., andButler, L.G. 1981. The specificity of proanthocyanidin-protein interactions.J. Biol. Chem. 256:4494–4497.

    PubMed  Google Scholar 

  • Jensen, R.G., andBahr, J.T. 1977. Ribulose-1,5-bisphosphate carboxylase-oxygenase.Annu. Rev. Plant Physiol. 28:379–400.

    Google Scholar 

  • Lyttleton, J.W. 1973. Proteins and nucleic acids.Chem. Biochem. Herb. 1:63–103.

    Google Scholar 

  • Martin, J.S.andMartin, M.M. 1982. Tannin assays in ecological studies: Lack of correlation between phenolics, proanthocyanidins and protein-precipitating constituents in mature foliage of six oak species.Oecologia 54:205–211.

    Google Scholar 

  • Martin, J.S., andMartin, M.M. 1983. Tannin assays in ecological studies. Precipitation of ribulose-1,5-bisphosphate carboxylase/oxygenase by tannic acid, quebracho, and oak foliage extracts.J. Chem. Ecol. 9:285–294.

    Google Scholar 

  • Martin, M.M., andMartin, J.S. 1984. Surfactants: Their role in preventing the precipitation of proteins by tannins in insect guts.Oecologia 61:342–345.

    Google Scholar 

  • McManus, J., Lilley, T.H., andHaslam, E. 1983. Plant polyphenols and their association with proteins, pp. 123–137,in P.A. Hedin (ed.). Plant Resistance to Insects. ACS Symposium Series 208. American Chemical Society, Washington, D.C.

    Google Scholar 

  • Oh, H., Hoff, J.E., Armstrong, G.S., andHaff, L.A. 1980. Hydrophobie interaction in tanninprotein complexes.J. Agric. Food Chem. 28:394–398.

    Google Scholar 

  • Rhoades, D.F., andCates, R.G. 1976. A general theory of plant antiherbivore chemistry.Recent Adv. Phytochem. 10:168–213.

    Google Scholar 

  • Schaffner, W., andWeissman, C. 1973. A rapid, sensitive and specific method for the determi- nation of protein in dilute solution.Anal. Biochem. 56:502–514.

    PubMed  Google Scholar 

  • Singer, E.J., Eggman, L., Campbell, J.M., andWildman, S.G. 1952. The proteins of green leaves. IV. A high molecular weight protein comprising a large part of the cytoplasmic protein.J. Biol. Chem. 197:233–239.

    PubMed  Google Scholar 

  • Swain, T. 1979. Tannins and lignins, pp. 657–682,in G.A. Rosenthal and D.H. Janzen (eds.). Herbivores: Their Interaction with Secondary Plant Metabolites. Academic Press, New York.

    Google Scholar 

  • Turunen, S., andKastari, T. 1979. Digestion and absorption of lecithin in larvae of the cabbage butterfly,Pieris brassicae.Comp. Biochem. Physiol. 62A:933–937.

    Google Scholar 

  • Van Sumere, C.F., Albrecht, J., Dedonder, A., Depooter, H., andPe, I. 1975. Plant protein and phenolics, pp. 211–264,in J.B. Harborne and C.F. Van Sumere (eds.). The Chemistry and Biochemistry of Plant Proteins. Academic Press, New York.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Martin, M.M., Rockholm, D.C. & Martin, J.S. Effects of surfactants, pH, and certain cations on precipitation of proteins by tannins. J Chem Ecol 11, 485–494 (1985). https://doi.org/10.1007/BF00989559

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00989559

Key words

Navigation