Human body odor consists of various kinds of odor components. Here, we have investigated the changes in body odor associated with aging. The body odor of subjects between the ages of 26 and 75 was analyzed by headspace gas chromatography/mass spectrometry. 2-Nonenal, an unsaturated aldehyde with an unpleasant greasy and grassy odor, was detected only in older subjects (40 y or older). Furthermore, analysis of skin surface lipids revealed that omega7 unsaturated fatty acids and lipid peroxides also increased with aging and that there were positive correlations between the amount of 2-nonenal in body odor and the amount of omega7 unsaturated fatty acids or lipid peroxides in skin surface lipids. 2-Nonenal was generated only when omega7 unsaturated fatty acids were degraded by degradation tests in which some main components of skin surface lipids were oxidatively decomposed using lipid peroxides as initiator of an oxidative chain reaction. The results indicate that 2-nonenal is generated by the oxidative degradation of omega7 unsaturated fatty acids, and suggest that 2-nonenal may be involved in the age-related change of body odor.

ABSTRACT-We investigated the effects of fragrance inhalation on sympathetic activity in normal adult subjects using both power spectral analysis of blood pressure fluctuations and measurement of plasma catecholamine levels. Fragrance inhalation of essential oils, such as pepper oil, estragon oil, fennel oil or grapefruit oil, resulted in 1.5-to 2.5-fold increase in relative sympathetic activity, representing low frequency amplitude of systolic blood pressure (SBP-LF amplitude), compared with inhalation of an odorless solvent, triethyl citrate (P<0.05, each). In contrast, fragrance inhalation of rose oil or patchouli oil caused a 40% decrease in relative sympathetic activity (P<0.01, each). Fragrance inhalation of pepper oil induced a 1.7-fold increase in plasma adrenaline concentration compared with the resting state (P = 0.06), while fragrance inhalation of rose oil caused a 30% decrease in adrenaline concentration (P<0.01). Our results indicate that fragrance inhalation of essential oils may modulate sympathetic activity in normal adults.Keywords: Sympathetic nerve function, Power spectral analysis, Catecholamine, Essential oil, Fragrance inhalationIt has been reported that olfactory stimulation by fragrance inhalation exerts various physiological effects on humans. Effects of fragrance on brain function have been studied by using alpha and theta activity in the electroencephalogram (EEG) (1) or contingent negative variation (CNV) (2, 3). These studies have shown that some fragrances exert stimulant or inhibitory effects on brain function. Moreover, it has been reported that human endocrine and immune systems are affected by fragrance in a study that assessed the effects of fragrance on both endocrine function, by analyzing urinary cortisol and dopamine levels, and immune function, by analyzing natural killer cell activity and CD4 /8 values (4).On the other hand, effects of fragrance on the autonomic nervous system have been studied by noninvasive recording of various autonomic parameters such as heart rate (HR), skin conductance and respiration (5), or skin temperature, skin conductance, breathing rate, pulse rate and blood pressure (6). To our knowledge, there is no study that has been designed to quantitate the separate effects of fragrances on sympathetic and parasympathetic activities.Power spectral analysis of heart rate variability or blood pressure fluctuations have been developed for the noninvasive assessment of autonomic nerve activity and utilized to assess the autonomic nerve activity in various disorders such as hypertension and diabetes mellitus (7 -9). In such analyses, it is assumed that the low frequency components (LF) of blood pressure fluctuations and the high frequency components (HF) of heart rate variability reflect sympathetic activity and parasympathetic activity, respectively (10). In general, fast Fourier transform processing has been employed for power spectral analysis of fluctuations, a new method, which provides real-time, noise-adjusted calculation of sympathetic and parasympat...

We constructed the plasmid pTTB151 in which the E. coli hioB gene was expressed under the control of the tac promoter. Conversion of dethiobiotin to biotin was demonstrated in cell-free extracts of E. coli carrying this plasmid. The requirements for this biotin-forming reaction included fructose-l,6-bisphosphate, Fe 2 +, S-adenosyl-L-methionine, NADPH, and KCI, as well as dethiobiotin as the substrate. The enzymes were partially purified from cell-free extracts by a procedure involving ammonium sulfate fractionation. Our results suggest that an unidentified enzyme(s) besides the hioB gene product is obligatory for the conversion of dethiobiotin to biotin.The involvement within the biotin biosynthetic pathway in E. coli of three enzymes, 7-keto-8-aminopelargonic acid synthetase,l) 7,8-diaminopelargonic acid aminotransferase,2,3) and dethiobiotin (DTB) synthetase 4 ,5) coded for by bioF, bioA, and bioD, respectively, has been demonstrated. It is also suggested that two other genes coded by bioC and bioH, whose functions still remain unclear, are involved in pimeloyl-CoA biosynthesis.6 ) In addition the enzyme encoded by bioB is believed to catalyze the conversion of DTB to biotin, the last step of biotin biosynthesis.

the enzymic conversion of dethiobiotin to biotin (catalyzed by the enzyme encoded by bioB) in cell-free extract of Escherichia coli which had been genetically engineered for high bioB expression. An unidentified protein(s) in addition to the bioB gene product is obligatory for this reaction. We have found that this protein was precipitated from the cell-free extract with poly(ethyleneimine), and we have purified it to homogeneity by a procedure which includes ammonium sulfate fractionation, DEAE-cellulose chromatography, gel filtration, and Mono Q chromatography. The apparent molecular mass of the purified protein was estimated to be about 21 kDa by SDSPAGE. The N-terminal amino acid sequence of the purified protein was identical with that of E. coli flavodoxin. We conclude that flavodoxin is required for conversion of dethiobiotin to biotin in E. coli. Studies with purified flavodoxin and the fraction containing the bioB gene product suggested that protein(s) in addition to the bioB gene product and flavodoxin is also obligatory for the reaction.

The origin of the carbon atoms of pimeloyl‐CoA, the earliest known precursor in the pathway of de novo biotin biosynthesis in Escherichia coli, was investigated by 13C‐NMR spectroscopy. In fermentation of the biotin‐overproducing DRK332/pXBA312 strain of Escherichia coli (a repressor mutant carrying a biotin operon fragment in the plasmid), a high dose of L‐alanine (8 g/l) stimulated dethiobiotin and biotin accumulation. Although L‐alanine is a known precursor of 7‐keto‐8‐aminopelargonic acid in biotin biosynthesis, the 13C‐NMR spectrum of dethiobiotin showed that the C‐3 of L‐[3‐13C]alanine was incorporated into not only the methyl carbon (C‐9) but also alternate carbons (C‐2, C‐4, C‐6) of the side chain, and these latter positions are the same as those labeled with D‐[1‐13C]glucose. These data indicate that L‐alanine can act as an alternative carbon source, suggesting that acetyl‐CoA is a possible precursor for pimeloyl‐CoA synthesis. In accordance with this hypothesis, the C‐1 of sodium (1‐13C)acetate and the C‐2 of sodium (2‐13C)acetate were incorporated into alternate carbons in the side chain of dethiobiotin, i.e., (C‐1, C‐3, C‐5, C‐7) and (C‐1, C‐2, C‐4, C‐6), respectively. These results suggested firstly that in E. coli pimeloyl‐CoA is biosynthesized from L‐alanine and/or acetate via acetyl‐CoA, but not via pimelic acid, which has been suggested as a biotin precursor in other species, and secondly that the carboxyl group of biotin originates from carbon dioxide produced through the tricarboxylic acid cycle.