Hostname: page-component-586b7cd67f-tf8b9 Total loading time: 0 Render date: 2024-11-22T20:46:48.487Z Has data issue: false hasContentIssue false
  • English
  • Français

Proanthocyanidins inhibit hydrolysis of leaf proteins by rumen microflora in vitro

Published online by Cambridge University Press:  10 October 2007

Gregory J. Tanner ,
Andrew E. Moore  and
Philip J. Larkin
Gregory J. Tanner
Affiliation:
Division of Plant Industry, Commonwealth Scientific and Industrial Research Organization, GPO Box 1600, Canberra, Australia
Andrew E. Moore
Affiliation:
Division of Plant Industry, Commonwealth Scientific and Industrial Research Organization, GPO Box 1600, Canberra, Australia
Philip J. Larkin
Affiliation:
Division of Plant Industry, Commonwealth Scientific and Industrial Research Organization, GPO Box 1600, Canberra, Australia
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Proanthocyanidins (condensed tannins; PA) purified from the leaves of forage legumes Trifolium arvense, Lotus pedunculatus, Lotus corniculatus, Dorycnium rectum, Coronilla varia, Onobrychis viciifolia, or Hedysarum coronarium, were added to soluble lucerne (Medicago sativa) leaf protein and incubated with strained rumen fluid in vitro. Fractions were collected and frozen immediately. Denatured proteins were fractionated by sodium dodecylsulphate–polyacrylamide gel electrophoresis (SDS–PAGE), stained, and relative levels were quantified by densitometry. In the absence of PA the large subunit (LSU) of ribulose bisphosphate carboxylase (EC 4. 1. 1. 39) was susceptible to proteolysis by rumen microflora but the small subunit (SSU) resisted breakdown. PA purified from Onobrychis was added to soluble leaf protein, at PA: protein ratios between 1:1 and 1:20. The rate of proteolysis of LSU1 was significantly reduced at PA: protein ratios of 1:2 and 1:1 (P < 0.001) and the rate of digestion was reduced by between 3- and 21-fold. In separate experiments PA isolated from the range of species described was added to rumen fluid to give PA: protein ratios of 1: 5. The addition of PA significantly reduced the rate of proteolysis of LSU, when compared with PA-free control. There were only small differences between PA from different species. The inhibitory effect of PA may have been due to PA binding to the dietary protein or to the rumen proteases, interfering with the action of proteases on susceptible sites within the substrate.

Keywords

Condensed tanninsProanthocyanidinsRumen microfloraIn vitro proteolysis
Type
Nutritional Effects of Plant Constituents
Information
British Journal of Nutrition , Volume 71 , Issue 6 , June 1994 , pp. 947 - 958
Copyright
Copyright © The Nutrition Society 1994

References

Asquith, T. N., & Butler, L. G. (1986). Interactions of condensed tannins with selected proteins. Phytochemistry 25, 1591–1593.CrossRefGoogle Scholar
Barry, T. N., Allsop, T. F. & Redekopp, C. (1986 a). The role of condensed tannins in the nutritional value of Lotus pedunculrrtus for sheep. British Journal of Nutrition 56, 607–614.CrossRefGoogle ScholarPubMed
Barry, T. N. & Duncan, S. J. (1984). The role ofcondensed tannins in the nutritional value of Lotuspedunculrctus for sheep. 1. Voluntary intake. British Journal of Nutrition 51, 485–491.CrossRefGoogle Scholar
Barry, T. N. & Manley, T. R. (1984). The role ofcondensed tannins in the nutritional value of Lotus peduncu1atus for sheep. 2. Quantitative digestion of carbohydrates and proteins. British Journal of Nutrition 51, 493–504.CrossRefGoogle Scholar
Barry, T. N. & Manley, T. R. (1986). Interrelationships between the concentrations of total condensed tannin, free condensed tannin and lignin in Lotus sp. and their possible consequences in ruminant nutrition. Journal of the Science of Food and Agriculture 37, 248–254.CrossRefGoogle Scholar
Barry, T. N., Manley, T. R. & Duncan, S. J. (1986 b). The role of condensed tannins in the nutritional value of Lotus pedunculatus for sheep. 4. Sites of carbohydrate and protein digestion as influenced by dietary reactive tannin concentration. British Journcil of Nutrition 55, 123–137.CrossRefGoogle ScholarPubMed
Broderick, G. A. & Clayton, M. K. (1992). Rumen protein degradation rates estimated by non-linear regression analysis of Michaelis-Menten in vitro data. British Journal of Nutrition 67, 27–42.CrossRefGoogle ScholarPubMed
Chiquette, J., Cheng, K. J., Costerton, J. W. & Milligan, L. P. (1988). Effect of tannins on the digestibility of two isosynthetic strains of birdsfoot trefoil (Lotus corniculatus L.) using in vitro and in sacco techniques. Canadian Journal of Animal Science 68, 751–760.CrossRefGoogle Scholar
Gray, J. C. (1982). Use of proteolytic inhibitors during isolation of plastid proteins. In Methods in Chloroplast Molecular Biology, pp. 1093–1102 [Edelman, M., editor]. Dublin: Elsevier Biomedical Press.Google Scholar
Horigome, T., Kumar, R. & Okamoto, K. (1988). Effects of condensed tannins prepared from leaves of fodder plants on digestive emzymes in vitro and in the intestine of rats. British Journal of Nutrition 60, 275–285.CrossRefGoogle Scholar
Jones, W. T., Broadhurst, R. B. & Lyttleton, J. W. (1976). The condensed tannins of pasture legume species. Phytochemistry 15, 1407–1409.CrossRefGoogle Scholar
Kristiansen, K. N. (1984). Biosynthesis of proanthocyanidins in barley: genetic control of the conversion of dihydroquercetin to catechin and procyanidins. Carlsberg Research Cornmunicutions 49, 503–524.CrossRefGoogle Scholar
Kumar, R. & Singh, M. (1984). Tannins, their adverse role in ruminant nutrition. Journal of Agricultural and Food Chemistry 32, 447–453.CrossRefGoogle Scholar
Kumar, R. & Vaithiyanathan, S. (1990). Occurrence, nutritional significance and effect on animal productivity of tannins in tree leaves. Animal Feed Science and Technology 30, 21–38.CrossRefGoogle Scholar
Laemmli, U. K. & Favre, M. (1973). Maturation of the head of bacteriophage T4. 1. DNA packaging events. Journal of Molecular Biology 80, 575–599.CrossRefGoogle Scholar
McDougall, E. I. (1948). Studies on ruminant saliva. 1. The composition and output of sheep's saliva. Biochemical Journal 43, 99–109.CrossRefGoogle ScholarPubMed
McLeod, M. N. (1974). Plant tannins - their role in forage quality. Nutrition Abstracts and Reviews 44, 803–815.Google Scholar
McManus, J. P., Davis, K. G., Lilley, T. H. & Haslam, E. (1981). The association of proteins with polyphenols. Journal of the Chemical Society Chemical Comniunications 7, 309–311.CrossRefGoogle Scholar
Mabry, T. J., Markham, K. R. & Thomas, M. B. (1970). The Systematic Identification of Flavonoids, pp. 3–14. New York: Springer-Verlag.CrossRefGoogle Scholar
Mangan, J. L. (1972). Quantitation studies on nitrogen metabolism in the bovine rumen. The rate of proteolysis of casein and ovalbumin and the release and metabolism of free amino groups. British Journal of Nutrition 27, 261 283.CrossRefGoogle Scholar
Martin, J. S. & Martin, M. M. (1983). Tannin assays in ecological studies: precipitation of ribulose-1,5,-bisphosphate carboxylase/oxygenase by tannic acid, qnebracho and oak foliage extracts. Journal of Chemical Eclogy 9, 285–294.Google ScholarPubMed
Mole, S. & Waterman, P. G. (1985). Stimulatory effects of tannins and cholic acid on tryptic hydrolysis of proteins: ecological implications. Journal of Chemical Ecology 11, 1323–1332.CrossRefGoogle ScholarPubMed
Petersen, J. C. & Hills, N. S. (1991). Enzyme inhibition by Sericea Lespedeza tannins and the use of supplements to restore activity. Crop Science 31, 827–832.CrossRefGoogle Scholar
Purchas, R. W. & Keogh, R. G. (1984). Fatness of lambs grazed on ‘Grasslands Maku’ lotus and ‘Grasslands Huia’ white clover. Proceedings of the New Zealand Socieiy of Animal Production 44, 219–221.Google Scholar
Rumbaugh, M. D. (1985). Breeding bloat-safe cultivars of bloat-causing legumes. In Forage Legumesfor Energy-eflicient Aninial Production. Proceedings of the Trilateral Workshop, Pailnerston North, N.Z., pp. 238–245 [Barnes, R.F., Ball, P. R., Bringham, R. W.Marten, G. C. and Minston, D. J., editors]. Washington, DC: USDA.Google Scholar
SpencerC. M. Ya, C. C. M. Ya, C., Martin, R, Gaffney, S. H, Goulding, P. N., Magnolato, D, Lilley, T. H., & Haslam, E. (1988). Polyphenol complexation some thoughts and observations. Phgtochemistrv 27, 2397–2409.CrossRefGoogle Scholar
Spencer, D., Higgins, T. J. V., Freer, M., Dove, H., & Coombe, J. B. (1988b). Monitoring the fate of dietary proteins in rumen fluid using gel electrophoresis. Briri.yh Journal of Nutrition 60, 241–247.CrossRefGoogle ScholarPubMed
Tagari, H, Henis, Y, & Volcani, R. (1965). Effect of carob pod extract on cellulolysis, proteolysis, deamination, and protein biosynthesis in an artificial rumen. Applied Microbiotog 13, 437–442.CrossRefGoogle Scholar
Van Hoven, W, & Furstenburg, D. (1992). The use of purified condensed tannin as a reference in determining its influence on rumen fermentation. Comparative Biochernistrv and Phvsiolopll 101 A. 381–385.CrossRefGoogle ScholarPubMed
Zucker, W. V. (1983). Tannins: does struchre determine function? An ecological perspective. American Naturalist 121. 335–365.CrossRefGoogle Scholar