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首页> 外文期刊>journal of applied toxicology >Complexing of toxic hydrolysable tannins of yellow‐wood (Terminalia oblongata) and harendong (Clidemia hirta) with reactive substances: An approach to preventing toxicity
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Complexing of toxic hydrolysable tannins of yellow‐wood (Terminalia oblongata) and harendong (Clidemia hirta) with reactive substances: An approach to preventing toxicity

机译:Complexing of toxic hydrolysable tannins of yellow‐wood (Terminalia oblongata) and harendong (Clidemia hirta) with reactive substances: An approach to preventing toxicity

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AbstractRuminants consuming either tannic acid or hydrolysable tannins from the Australian yellow‐wood tree (Terminalia oblongata) and the Indonesian shrubClidemia hirtaare intoxicated by simple phenolics liberated in the gut. The affinity of these tannins and of the simple phenolic gallic acid for the two proteins casein and pepsin, polyvinylpyrolidone (PVP), activated charcoal and Ca(OH)2was examinedin vitro.The studies were undertaken to predict the effect of these phenolics on digestion and to identify substances that would act as antidotes by precipitating phenolics. Tannins but not gallic acid were precipitated as stable complexes with both pepsin and casein at pH 3–5. Optimal complexing of tannin with protein occurred at a weight ratio of 1:1. Ionic strength and temperature did not affect the amount of tannin precipitated from solution with protein. The precipitation of tannins with PVP and Ca(OH)2was unaffected by pH within the range 2–8 while maximum binding with activated charcoal occurred between pH 3 and 7. In contrast to protein, the other substances complexed with gallic acid; only gallic acid‐PVP complexess were affected by pH. Calcium hydroxide bound more tannin and gallic acid on a weight basis than PVP and charcoal. Both Ca(OH)2and activated charcoal should complex with phenolics in the forestomach, abomasum and intestines.The reaction of hydrolysable tannins and proteins at the pH found in the abomasum suggests that hydrolysable tannins would interfere with enzyme function and protein digestion post‐ruminally rather than in the fo

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