The reaction of tannin fractions isolated from the bark of Betula, Salix, and Pinus species with two enzymes, β-glucosidase and esterase, was investigated. The influence of precipitation to the hydrolytic capacity of β-glucosidase also was studied. All tannins studied precipitated β-glucosidase and esterase, and moderate differences in the precipitating capacities of the tannins were observed. Interestingly, complex formation between β-glucosidase and tannin did not markedly affect the activity of the enzyme. Therefore, complex formation during the insect/herbivore feeding does not necessarily change the defense activity of phenolic glycosides or decrease activity of digestive enzymes.
This is a preview of subscription content, access via your institution.
Buy single article
Instant access to the full article PDF.
Price includes VAT (USA)
Tax calculation will be finalised during checkout.
Amory, A. M., and Schubert, C. L. 1987. A method to determine tannin concentration by the measurement and quantification of protein–tannin interactions. Oecologia 73:420–424.
Ayres, M. P., Clausen, T. P., Maclean, S. F., Jr., Redman, A. M., and Reichardt, P. B. 1997. Diversity of structure and antiherbivore activity in condensed tannins. Ecology 78:1696–1712.
Becker, P., and Martin, J. S. 1982. Protein-precipitating capacity of tannins in Shorea (Dipterocarpaceae) seedling leaves. J. Chem. Ecol. 8:1353–1367.
Bernays, E. A., Cooper Driver, G., and Bilgener, M. 1989. Herbivores and plant tannins. Adv. Ecol. Res. 19:263–302.
Bradford, M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72:248–254.
Butler, L. G., Price, M. L., and Brotherton, J. E. 1982. Vanillin assay for proanthocyanidins (condensed tannins): Modification of the solvent for estimation of the degree of polymerization. J. Agric. Food Chem. 30:1087–1089.
Clausen, T. P., Reichardt, P. B., Bryant, J. P., WERNER, R. A., Post, K., and Frisby, K. 1989. Chemical model for short-term induction in quaking aspect (Populus tremuloides) foliage against herbivores. J. Chem. Ecol. 15:2335–2346.
Esen, A. 1993. α-Glucosidases: Overview, pp. 1–14, in A. Esen (ed.). β-Glucosidases: Biochemistry and Molecular Biology. American Chemical Society, Washington, D.C.
Goldstein, W. S., and Spencer, K. C. 1985. Inhibition of cyanogenesis by tannins. J. Chem. Ecol. 11:847–858.
Goldstein, J. L., and Swain, T. 1965. The inhibition of enzymes by tannins. Phytochemistry 4:185–192.
Gopalan, V., Pastuszyn, A., Galey, W. R., JR., and Glew, R. H. 1992. Exolytic hydrolysis of toxic plant glucosides by guinea pig liver cytosolic β-glucosidase. J. Biol. Chem. 267:14027–14032.
GUYOT, S., Pellerin, P., Brillouet, J.-M., and Cheynier, V. 1996. Inhibition of β-glucosidase (Amygdalae dulces) by (+)-catechin oxidation products and procyanidin dimers. Biosci. Biotech. Biochem. 60:1131–1135.
Hagerman, A. E. 1989. Chemistry of tannin-protein complexation, pp. 323–334, in R. W. Hemingway and J. J. Karchesy (eds.). Chemistry and Significance of Condensed Tannins. Plenum Press, New York.
Hagerman, A. E., and Butler, L. G. 1978. Protein precipitation method for the quantitative determination of tannins. J. Agric. Food Chem.26:809–812.
Haslam, E. 1974. Polyphenol-protein interactions. Biochem. J. 139:285–288.
Julkunen-Tiitto, R. 1985. Phenolic constituents in the leaves of northern willows: Methods for the analysis of certain phenolics. J. Agric. Food Chem. 33:213–217.
Julkunen-Tiitto, R., and Meier, B. 1992. The enzymatic decomposition of salicin and its derivatives obtained from Salicaceae species. J. Nat. Prod. 55:1204–1212.
Julkunen-Tiitto, R., Petersen, M., Meinhard, J., and Alferman, A. W. A. 1996. Characterization of novel salicin glucosyltranferase from willow (Salix sp.) cell cultures. International Symposium on Principles Regulating Biosynthesis and Storage of Secondary Products. Halle.
Juntheikki, M.-R., Julkunen-tiitto, R., and Hagerman, A. E. 1996. Salivary tannin-binding proteins in root vole (Microtus oeconomus Pallas). Biochem. Syst. Ecol. 24:25–35.
Kawamoto, H., Mizutani, K., and Nakatsubo, F. 1997. Binding nature and denaturation of protein during interaction with galloylglucose. Phytochemistry 46:473–478.
Kolehmainen, J., Roininen, H., Julkunen-Tiitto, R., and TAHVANAINEN, J. 1994. Importance of phenolic glucosides in host selection of the shoot galling sawfly, Euura amerinae, on Salix pentandra. J. Chem. Ecol. 20:2455–2466.
Kolodziej, H. 1989. Procyanidins from medicinal birch: bonding patterns and sequence of units in triflavonoids of mixed stereochemistry. Phytochemistry 28:3487–3492.
Kolodziej, H. 1990. Oligomeric flavan-3-ols from medicinal willow bark. Phytochemistry 29:955–960.
KÖph, A., Rank, N. E., Roininen, H., Julkunen-Tiitto, R., Pasteels, J. M., and Tahvanainen, J. 1998. Phylogeny and the evolution of host plant use and sequestration in the willow leaf beetle genus Phratora (Coleoptera: Chrysomelidae). Evolution 52:517–528.
Kumar, R., and Horigome, T. 1986. Fractionation, characterization, and protein-precipitating capacity of the condensed tannins from Robinia pseudo acacia L. leaves. J. Agric. Food Chem. 34:487–489.
Kumar, R., and Singh, M. 1984. Tannins: Their adverse role in ruminant nutrition. J. Agric. Food Chem. 32:447–453.
Martin, J. S., and Martin, 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.
Matthews, S., Mila, I., Scalbert, A., and Donnelly, D. M. 1997. Extractable and non-extractable proanthocyanidins in barks. Phytochemistry 45:405–410.
Ozawa, T., Lilley, T. H., and Haslam, E. 1987. Polyphenol interactions: Astringency and the loss of astringency in ripening fruit. Phytochemistry 26:2937–2942.
Rank, N. E., KÖph, A., Julkunen-Tiitto, R., and Tahvanainen, J. 1998. Host performance and larval performance of the salicylate-using leaf beetle Phratora vitellinae. Ecology 79:618–631.
Reichardt, P. B., Clausen, T. P., and Bryant, J. P. 1988. Phenol glycosides in plant defense against herbivores, pp. 130–142, in H. G. Cutler (ed.). Biologically Active Natural Products, Potential Use in Agriculture. American Chemical Society, Washington, D.C.
Reichardt, P. B., Bryant, J. P., Mattes, B. R., Clausen, T. P., Chapin, F. S., III, and Meyer, M. 1990. Winter chemical defense of alaskan balsam poplar against snowshoe hares. J. Chem. Ecol. 16:1941–1959.
Selmar, D. 1993. Apoplastic occurrence of cyanogenic β-glucosidases and consequences for the metabolism of cyanogenic glucosides, pp. 191–204, in A. Esen (ed.). β-Glucosidases: Biochemistry and Molecular Biology. American Chemical Society, Washington, D.C.
Spencer, C. M., Cai, Y., Martin, R., Gaffney, S. H., Goulding, P. N., Magnolato, D., Lilley, T. H., and Haslam, E. 1988. Polyphenol complexation—some thoughts and observations. Phytochemistry 27:2397–2409.
Tahvanainen, J., Helle, E., Julkunen-Tiitto, R., and Lavola, A. 1985. Phenolic compounds of willow bark as deterrents against feeding by mountain hare. Oecologia 65:319–323.
Waterman, P. G., and Mole, S. 1994. Analysis of Phenolic Plant Metabolites. Blackwell Scientific Publications, Oxford.
Williams, V. M., Porter, L. J., and Hemingway, R. W. 1983. Molecular weight profiles of proanthocyanidin polymers. Phytochemistry 22:569–572.
About this article
Cite this article
Juntheikki, MR., Julkunen-Tiitto, R. Inhibition of β-Glucosidase and Esterase by Tannins from Betula, Salix, and Pinus Species. J Chem Ecol 26, 1151–1165 (2000). https://doi.org/10.1023/A:1005427809812
- condensed tannins
- enzyme inhibition
- protein precipitation
- defense activity