Extracts of common buckwheat bran prevent sucrose digestion.
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Buckwheat has been shown to have various health benefits such as reduction of hypertension and improvement of hypercholesterolemia; however, its effect on diabetes has not been fully elucidated. In this study, buckwheat bran extracts (BBE) inhibited sucrase activity in vitro more effectively than buckwheat. Balb/c mice pretreated with BBE showed dose-dependent reductions of blood glucose, greater than those observed with control mice, within 60 min following oral sucrose administration. Blood glucose levels in mice pretreated with buckwheat extracts were also significantly lower compared to those in control mice within 30 min following oral administration of sucrose. However, rutin, one of the abundant polyphenols of BBE, did not lower blood glucose level. Our data indicate that components of BBE other than rutin have inhibitory activity against sucrase in vivo. These results suggest that BBE could have beneficial effects on diabetes. (+info)
Fagopyrum tataricum (buckwheat) improved high-glucose-induced insulin resistance in mouse hepatocytes and diabetes in fructose-rich diet-induced mice.
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Differential transcript profiling through cDNA-AFLP showed complexity of rutin biosynthesis and accumulation in seeds of a nutraceutical food crop (Fagopyrum spp.).
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Identification of a new IgE-binding epitope of peanut oleosin that cross-reacts with buckwheat.
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Peanut and buckwheat induce a severe allergic reaction, anaphylaxis, which is considered to be mediated by immunoglobulin E (IgE). We identified in this study a new IgE-binding epitope of the peanut allergen that cross-reacted with buckwheat. The phosphate-buffered saline-soluble fraction of buckwheat inhibited the binding between IgE and the peanut allergen. A cross-reactive peptide was isolated from the alpha-chymotrypsin hydrolysate of peanut. Based on the amino acid sequence and mass spectrometric analysis data, the peptide was identified as Ser-Asp-Gln-Thr-Arg-Thr-Gly-Tyr (SDQTRTGY); this sequence is identical to amino acids 2-9 in the N-terminal hydrophilic domain of oleosin 3 which is located on the surface of the lipid storage body. Synthetic SDQTRTGY was found to bind with IgE in the sera of all eight peanut-allergic patients tested. Since many foods of plant origin contain oleosin, the possibility of an anaphylactic cross-reaction in allergic patients should always be considered. (+info)