Hostname: page-component-cd9895bd7-8ctnn Total loading time: 0 Render date: 2024-12-28T20:50:11.936Z Has data issue: false hasContentIssue false
  • English
  • Français

Adaptation of cattle to tannins: rôle of proline-rich proteins in oak-fed cattle

Published online by Cambridge University Press:  02 September 2010

H. P. S. Makkar  and
K. Becker
H. P. S. Makkar
Affiliation:
University of Hohenheim, Institute for Animal Production in the Tropics and Subtrapics (480), Department of Animal Nutrition and Aquaculture, D-70593 Stuttgart, Germany
K. Becker
Affiliation:
University of Hohenheim, Institute for Animal Production in the Tropics and Subtrapics (480), Department of Animal Nutrition and Aquaculture, D-70593 Stuttgart, Germany
Get access

Abstract

Saliva and faecal samples were collected from hill cattle (no. = 10) given tannin-rich oak (Quercus incana) leaves in the north-west Himalayan region of India. Amino acid composition of the saliva samples after thawing to remove precipitated proteins by centrifugation, and dialysis (molecular weight cut off: 3500) to remove small moieties revealed 6·4 (s.d. 0·6) % proline, 15·6 (s.d. 0·6) % glutamine plus glutamate and 9·2 (s.d. 1·0) % glycine on molar basis. For Holstein Friesian cattle (no. = 4) which had no history of consumption of tannin-containing foods, these values were 6·5 (s.d. 0·4) %, 15·2 (s.d. 0·5) % and 9·8 (s.d. 0·7) % respectively. Proline concentration in the proteins present either as free or as tannin-protein complexes in the lyophilized faecal samples from hill cattle was 4·7 (s.d. 0·2) % (on molar basis) of the total amino acids and 5·3 (s.d. 0·2) % in Holstein Friesian cattle. In the faeces of oak-fed cattle, the tannin and condensed tannin levels on dry-weight basis were 0·81 (s.d. 0·20) % as tannin acid equivalent and 0·06 (s.d. 0·04) % as leucocyanidin equivalent respectively. For tannic acid, the relative affinity of salivary proteins, using the competitive binding assay, was about six-times higher than that of bovine serum albumin (BSA) and was of the same order as that of gelatin. Turbidity of complexes formed between salivary proteins or BSA and tannic acid showed proportionately about 0·50 lower turbidity for salivary proteins in 0-2 mol/I acetate buffer (pH 4·9 containing 0·17 mol/l NaCl) and proportionately about 0·84 lower turbidity in distilled water. The results suggest that unlike rats or mice, the proline-rich proteins do not appear to be of any physiological significance in the adaptation of cattle to tannins. However, the salivary proteins of cattle though not rich in proline, have a high affinity for tannins and these proteins have a high tendency to form soluble tannin-protein complexes.

Keywords

cattleoak leavesprolinesalivatannins
Type
Research Article
Information
Animal Science , Volume 67 , Issue 2 , October 1998 , pp. 277 - 281
Copyright
Copyright © British Society of Animal Science 1998

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Arafa, A., Ashoub, A. and Hussein, L. 1989. Faba bean proanthocyanidin in human nutrition and its effect on the induction of salivary proline-rich proteins. Bulletin of the Egypt Society of Physiological Science 9:269–281.Google Scholar
Asquith, T. N. and Butler, L. G. 1985. Use of dye-labeled protein as spectrophotometric assay for protein precipitants such as tannin. Journal of Chemical Ecology 11:1535.CrossRefGoogle ScholarPubMed
Asquith, T. N., Uhlig, J., Mehansho, H., Putman, L., Carlson, D. M. and Butler, L. 1987. Binding of condensed tannins to salivary protein-rich glycoproteins: the role of carbohydrate. Journal of Agricultural and Food Chemistry 35: 331–334.CrossRefGoogle Scholar
Austin, P. J., Sucher, L. A., Robbins, C. T. and Hagerman, A. E. 1989. Tannin-binding proteins in saliva of deer and their absence in saliva of sheep and cattle. Journal of Chemical Ecology 15:1335–1347.CrossRefGoogle ScholarPubMed
Bejovic, S., Duzic, E., Sacirbrebegovic, A. and Tafro, A. 1978. Examination of variations of tannase activity in ruminal content and mucosa of goats on oak leaf diet and during intraruminal administration of 3 to 10% tannic acid. Veterinarya, Sarajevo 27:445–457.Google Scholar
Dietz, B. A., Hagerman, A. E. and Barrett, G. W. 1994. Role of condensed tannin on salivary tannin-binding proteins, bioenergetics, and nitrogen digestibility in Microtus pennsylvanicus. Journal of Mammalogy 75:880–889.CrossRefGoogle Scholar
Distel, R. A. and Provenza, F. D. 1991. Experience early in life affects voluntary intake of blackbrush by goats. Journal of Chemical Ecology 17:431–450.CrossRefGoogle ScholarPubMed
Eggum, B. O. and Christensen, K. D. 1975. Influence of tannin on protein utilization in feedstuffs with special reference to barley. In Breeding for seed protein improvement using nuclear techniques, IAEA-PL-570/10, pp. 135–143. International Atomic Energy Agency, Vienna.Google Scholar
Fürst, P., Pollack, L., Graser, T. A., Godel, H. and Stehle, P. 1990. Appraisal of four pre-column derivatization methods for the high performance liquid chromatographic determination of free amino acids in biological materials. Journal of Chromatography 499:557–569.CrossRefGoogle ScholarPubMed
Hagerman, A. E. and Butler, L. G. 1978. Protein precipitation method for the quantitative determination of tannins. Journal of Agricultural and Food Chemistry 26: 809–812.CrossRefGoogle Scholar
Jansman, A. J. M. 1993. Tannins in faba beans (Viciafaba L.) — antinutritional properties in monogastric animals. Ph.D. thesis, Wageningen Agricultural University.Google Scholar
Jansman, A. J. M., Frohlich, A. A. and Marquardt, R. R. 1994. Production of proline-rich proteins by the parotid glands of rats is enhanced by feeding diets containing tannins from faba beans (Vicia faba L.). Journal of Nutrition 124: 249–258.CrossRefGoogle ScholarPubMed
Jansman, A. J. M., Verstegen, M. W. A., Huisman, J. and Berg, J. W. O. van den. 1995. Effects of hulls of faba bean (Vicia faba L.) with a low or high content of condensed tannins on the apparent ileal and fecal digestibility of nutrients and the excretion of endogenous protein in ileal digesta and feces of pigs. Journal of Animal Science 73: 118–127.CrossRefGoogle ScholarPubMed
Magné, C. and Larher, F. 1992. High sugar content of extracts interferes with colorimetric determination of amino acids and free proline. Analytical Biochemistry 200:115–118.CrossRefGoogle ScholarPubMed
McArthur, C., Sanson, G. D. and Beal, A. M. 1995. Salivary proline-rich proteins in mammals: role in oral homeostasis and counteracting dietary tannin. Journal of Chemical Ecology 21: 663–691.CrossRefGoogle Scholar
Makkar, H. P. S. 1993. Antinutritional factors in foods for livestock. In Animal production in developing countries (ed. Gill, M., Owen, E., Pollott, G. E. and Lawrence, T. L. J.), British Society of Animal Production, occasional publication no. 16, pp. 69–95.Google Scholar
Makkar, H. P. S., Blümmel, M., Borowy, N. K. and Becker, K. 1993. Gravimetric determination of tannins and their correlations with chemical and protein-precipitation methods. Journal of the Science of Food and Agriculture 61: 161–165.CrossRefGoogle Scholar
Mehansho, H., Butler, L. G. and Carlson, D. M. 1987. Dietary tannins and salivary proline-rich proteins: interactions, induction, and defense mechanisms. Annual Review of Nutrition 7:423–440.CrossRefGoogle ScholarPubMed
Mehansho, H. and Carlson, D. M. 1983. Induction of protein and glycoprotein synthesis in rat- submandibular glands by isoproterenol. Journal of Biological Chemistry 258: 6616–6620.CrossRefGoogle ScholarPubMed
Mehansho, H., Clements, S., Sheares, B. T., Smith, S. and Carlson, D. M. 1985. Induction of proline-rich glycoprotein synthesis in mouse salivary glands by isoproterenol and by tannins. Journal of Biological Chemistry 260:4418–4423.CrossRefGoogle ScholarPubMed
Mehansho, H., Hagerman, A. E., Clements, S., Butler, L., Rogler, J. and Carlson, D. M. 1983. Modulation of proline-rich protein biosynthesis in rat parotid glands by sorghum with high tannin levels. Proceedings of the National Academy of Sciences of the United States of America 80: 3948–3952.CrossRefGoogle ScholarPubMed
Mitaru, B. N., Reichert, R. D. and Blair, R. 1984. The binding of dietary protein by sorghum tannins in the digestive tract of pigs. Journal of Nutrition 114:1787–1796.CrossRefGoogle ScholarPubMed
Mole, S., Butler, L. G. and Iason, G. 1990. Defense against dietary tannins in herbivores: a survey for proline-rich salivary proteins in mammals. Biochemical Systematics and Ecology 18:287–293.CrossRefGoogle Scholar
Porter, L. J., Hrstich, L. N. and Chan, B. C. 1986. The conversion of procyanidins and prodelphidins to cyanidin and delphinidin. Phytochemistry 25: 223–230.CrossRefGoogle Scholar
Robbins, C. T., Hagerman, A. E., Austin, P. J., McArthur, C. and Hanley, T. A. 1991. Variation in mammalian physiological responses to a condensed tannin and its ecological implications. Journal of Mammalogy 72:480–486.CrossRefGoogle Scholar
Robbins, C. T., Mole, S., Hagerman, A. E. and Hanley, T. A. 1987. Role of tannins in defending plants against ruminants: reduction of dry matter digestion? Ecology 68: 1606–1615.CrossRefGoogle ScholarPubMed
Schulz, G. E. and Schirmer, R. H. 1979. Principles of protein structure. Springer, New York.CrossRefGoogle Scholar
Troll, W. and Lindsley, J. 1955. A photometric method for the determination of proline. Journal of Biological Chemistry 215: 655–660.CrossRefGoogle ScholarPubMed
Yang, C. M. J. and Russell, J. B. 1992. Persistence of proline-containing peptides to ruminal degradation in vitro. Applied and Environmental Microbiology 58:3954–3958.CrossRefGoogle Scholar