LG1 (38.6 g/L), compared to LG2 (24.9 g/L). The maximum ATP production was observed early in the SSF process. LG1 revealed higher potential as substrate for ethanol production.

No abstract

Hydrolyzate of wheat bran hemicellulose was demonstrated to stimulate significantly the growth of bifidobacteria in the ceca of Wistar rats and ICR mice fed the purified diets including the hydrolyzate at 2.5% and 5.0% for 4 weeks. In contrast, Enterobacteriaceae, viridans streptococci, and staphylococci were decreased in numbers, especially at 5.0% level of the hydrolyzate. Lactobacilli were slightly increased in numbers, but not significantly, in mice. No significant changes were found in the numbers of the other examined microbes. The cecal concentrations of total short-chain fatty acids and acetic and propionic acids increased remarkably in both the animals in proportion to the rate of the hemicellulose hyrolyzate contained in the diets while those of iso-butyric and iso-valeric acids decreased. The butyric acid concentration increased in mice but not in rats. The cecal pH values were inversely proportional to the total concentrations of short-chain fatty acids.

Bamboo hemicellulose hydrolysate (BHH) was extracted from bamboo by high temperature and enzymatic treatment. The ratio of total sugars in BHH was 75.7% on a dry matter basis (sugar components: 46.4% glucose, 12.7% arabinose, 40.9% xylose). These were mainly comprised of low molecular weight oligosaccharides containing ferulic acid. BHH exhibited strong anti-oxidative activities. In high fat (HF) diet-fed mice, 5% BHH supplementation significantly ameliorated increases in plasma cholesterol levels compared to the control mice fed HF diet alone. Also, while the fecal pH of control mice increased, that of test mice (5% BHH supplementation) did not increase to similar levels. Greater amounts of propionic acid were detected in the feces of HF diet-fed mice fed HF supplemented with BHH than one fed HF diet alone.

The adenylation domain of nonribosomal peptide synthetase (NRPS) is responsible for its selective substrate recognition and activation of the substrate (yielding an acyl-O-AMP intermediate) on ATP consumption. DhbF is an NRPS involved in bacillibactin synthesis and consists of multiple domains [adenylation domain, condensation domain, peptidyl carrier protein (PCP) domain, and thioesterase domain]; DhbFA1 and DhbFA2 (here named) are "internal" adenylation domains in the multidomain enzyme DhbF. We firstly succeeded in expressing and purifying the "internal" adenylation domains DhbFA1 and DhbFA2 separately. Furthermore, we initially demonstrated dipeptide synthesis by "internal" adenylation domains. When glycine and L-cysteine were used as substrates of DhbFA1, the formation of N-glycyl-L-cysteine (Gly-Cys) was observed. Furthermore, when L-threonine and L-cysteine were used as substrates of DhbFA2, N-L-threonyl-L-cysteine (Thr-Cys) was formed. These findings showed that both adenylation domains produced dipeptides by forming a carbon-nitrogen bond comprising the carboxyl group of an amino acid and the amino group of L-cysteine, although these adenylation domains are acid-thiol ligase using 4'-phosphopantetheine (bound to the PCP domain) as a substrate. Furthermore, DhbFA1 and DhbFA2 synthesized oligopeptides as well as dipeptides.