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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
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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

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