No abstract

No abstract

Tolerance to bitter foods and its potentiation by repetitive exposure are commonly experienced and potentially underlie the consumption of bitter foods, but it remains unknown whether permissive and adaptive responses are general phenomena for bitter-tasting substances or specific to certain substances, and they have not been rigorously studied in mice. Here, we investigated the effects of prolonged exposure to a bitter compound on both recognition and rejection behaviors to the same compound in mice. Paired measurements of rejection (RjT) and apparent recognition (aRcT) thresholds were conducted using brief-access two-bottle choice tests before and after taste aversion conditioning, respectively. First, RjT was much higher than aRcT for the bitter amino acids L-tryptophan and L-isoleucine, which mice taste daily in their food, indicating strong acceptance of those familiar stimuli within the concentration range between RjT and aRcT. Next, we tested five other structurally dissimilar bitter compounds, to which mice were naive at the beginning of experiments: denatonium benzoate, quinine-HCl, caffeine, salicin, and epigallocatechin gallate. RjT was moderately higher than aRcT for all the compounds tested, indicating the presence of innate acceptance to these various, unfamiliar bitter stimuli in mice. Lastly, a 3-week forced exposure increased RjT for all the bitter compounds except salicin, demonstrating that mice acquire tolerance to a broad array of bitter compounds after long-term exposure to them. Although the underlying mechanisms remain to be determined, our studies provide behavioral evidence of innate and acquired tolerance to various bitter stimuli in mice, suggesting its generality among bitterants.

No abstract

The properties of soya bean proteins following y-irradiation (5-20 kGy) were investigated in connection with protein denaturation. Irradiation doses above 10 kGy caused a decrease in 7s and 11s components and an increase in 2s and 15s components (P < 0.05). However, subunit patterns determined by electrophoresis were not changed appreciably over the entire irradiation dose range. In the differential scanning calorimetry thermogram, the denaturation temperatures of 11s and 7s components were not affected by yirradiation, while increased irradiation dose caused a decrease in the enthalpy values of 11s and 7s components due to protein denaturation. Changes in the circular dichroism spectra and tryptophan fluorescence intensity (P < 0.05) were observed only at 20 kGy.