Whole quinoa grain was separated into bran and milled grain, and the milled grain into perisperm and embryo. The proximate composition of the milled grain was similar to that of whole grain. The protein and lipid content of the embryo was 57% of total protein and 49% of total lipid, respectively. Mineral analysis showed that the quinoa grain was rich in K, Mg, Ca, P and Fe. The perisperm contained large oval starch aggregates 20-30 m in diameter and polygonal granules around 1 m in diameter. Differential scanning calorimetry data indicated a gelatinization temperature of 54.0 to 71.0˚C and enthalpy of 11.0 J/g starch. The water-soluble protein and NaCl-soluble protein fractions composed 28.7-36.2% and 28.9-32.9% of total protein in each fraction. Unsaturated fatty acid accounted for 87.2-87.8% of total fatty acid. Phytate, a trypsin inhibitor activity and lipoxygenase activity in the embryo were highest. The saponin content of the bran was 86% of total saponin.

BackgroundEssential oils are often used in alternative medicine as analgesic and anti-inflammatory remedies. However, the specific compounds that confer the effects of essential oils and the molecular mechanisms are largely unknown. TRPM8 is a thermosensitive receptor that detects cool temperatures and menthol whereas TRPA1 is a sensor of noxious cold. Ideally, an effective analgesic compound would activate TRPM8 and inhibit TRPA1.ResultsWe screened essential oils and fragrance chemicals showing a high ratio of human TRPM8-activating ability versus human TRPA1-activating ability using a Ca2+-imaging method, and identified 1,8-cineole in eucalyptus oil as particularly effective. Patch-clamp experiments confirmed that 1,8-cineole evoked inward currents in HEK293T cells expressing human TRPM8, but not human TRPA1. In addition, 1,8-cineole inhibited human TRPA1 currents activated by allyl isothiocyanate, menthol, fulfenamic acid or octanol in a dose-dependent manner. Furthermore, in vivo sensory irritation tests showed that 1,8-cineole conferred an analgesic effect on sensory irritation produced by TRPA1 agonists octanol and menthol. Surprisingly, 1,4-cineole, which is structurally similar and also present in eucalyptus oil, activated both human TRPM8 and human TRPA1.Conclusions1,8-cineole is a rare natural antagonist of human TRPA1 that has analgesic and anti-inflammatory effects possibly due to its inhibition of TRPA1.

We found that lysophospholipase D (LPLD) in rat plasma prefers unsaturated to saturated lysophosphatidylcholines as substrates, generating a biologically active lipid, lysophosphatidic acid, but it does not hydrolyze diacyl-phospholipids. In this study, this LPLD required a metal ion for activity, Co2+ being the most effective, followed in order by Zn2+, Mn2+, and Ni2+. This metal-ion-stimulated LPLD with unique substrate specificity, which has not been described previously, was susceptible to thiol-blocking reagents and serine esterase inhibitors, but not to a histidine-modifying reagent. Consistent with results using thiol-modifying agents, short-chain fatty aldehydes, secondary products of lipid peroxidation, were found to inhibit LPLD. Addition of dibutylhydroxytoluene or butylhydroxyanisole to the plasma increased the activity of this enzyme, probably in a manner independent of its antioxidant activity, since another antioxidant, propyl gallate, was rather inhibitory. These results suggest that rat plasma contains an active LPLD that differs in some properties from other members of the known phospholipase D family detected in animal tissues and body fluids.

Three thiamine‐binding proteins of 17‐19 kDa (STBP‐I, II, and III) were purified from sesame seed (Sesamum indicum L.). Each of the proteins was composed of two subunits of equal molecular mass and each subunit consisted of a large polypeptide and a small polypeptide linked by a disulfide bond(s). They were rich in glutamic acid (or glutamine) and arginine. Their binding activities were optimal at neutral pH. They bound specifically free thiamine but not thiamine phosphates. STBP‐I had higher affinity for thiamine than STBP‐II or STBP‐III. STBP‐II and STBP‐III bound one molecule of thiamine per molecule, and STBP‐I bound 0.5 molecule. The amino acid composition and structure of the STPBs were similar to those of 2S storage proteins.