Formation of non-graphitizable isotropic spherulitic carbon from poly-divinylbenzene by pressure pyrolysis

Isotropic spherulites of carbon stable at 2000° C were synthesized by the pressure pyrolysis of divinylbenzene polymer sealed in a capsule. The morphology of the synthesized carbon was pressure and temperature dependent being influenced by the state of polymerization of the starting polymer. Using a polymer prepared at atmospheric pressure and 150° C without catalyst, isolated spherulitic carbon was formed at 700° C and pressures of 1000 to 1250 kg cm^–2. These spherulitic carbons were optically isotropic, hard and non-graphitizable after heat treatment at 2000° C. Such carbons originate in the co-existence of higher and lower molecular weight products of pressure pyrolysis and the survival cross-linkages in the original polymer.     

Syntheses of functional condensation polymers. II. A polyamide having epoxy groups and its ring-opening derivatives

Polyamides having epoxy groups and their ring-opening derivatives were prepared and characterized, and some of their properties were investigated. Reaction conditions for the low-temperature polycondensation of cis-2,3-epoxysuccinyl chloride (ESC) with aromatic diamines and the interfacial copolycondensation of ESC and adipyl chloride (AC) with aromatic diamines were established to obtain a high molecular weight polyamide having epoxy groups. In addition, the ring-opening reactions of the epoxy groups in the polyamides were carried out with various amines in order to obtain polyamides having hydrophilic pendent groups such as amino and hydroxyl. It was found that the polyamides prepared by ring-opening reaction of the epoxy group with ethylenediamine (EDA) or ethanolamine (EA) had a higher affinity for moisture than those with hexamethylenediamine (HMD) or n-butylamine (n-BA), which might be ascribed to the distance of hydrophilic groups from the polyamide chain. Those polyamides having hydrophilic pendent groups decomposed upon heating at less than 200°C.     

Disappearance of aromatic hydrocarbons and organic sulfur compounds from fish flesh reared in crude oil suspension

Eels (Anguilla Japonica Temminck et Schlegel) were reared in sea water containing a crude oil suspension (50 ppm for 10 days for aromatic hydrocarbons, 2500 ppm for 3 days for organic sulfur compounds), then transferred to clean sea water. The disappearance of aromatic hydrocarbons and organic sulfur compounds from eel flesh was examined. The concentration ratio (concentration of eel flesh/concentration of water) of benzene, toluene, m- or p-xylene and o-xylene at 10 days was 3.5, 13.2, 23.6 and 21.4 respectively.Benzene, toluene, m- or p-xylene and o-xylene disappeared after the transfer to clean sea water, and the half-life period was 0.5, 1.4, 2.6 and 2.0 days respectively in the first phase which lasted 0–5 days.Organic sulfur compounds in cel flesh decreased as the time spent in clean sea water increased, but were still present after 30 days.The results suggest that aromatic hydrocarbons and organic sulfur compounds could serve as markers of oil pollution in fish.     

Molecular Design and Synthesis of a Novel Substrate for Assaying Lysozyme Activity

A novel substrate {Galβ1,4GlcNAcβ1,4GlcNAc-β-pNP [Gal(GlcNAc)₂-β-pNP]} for assaying lysozyme activity has been designed using docking simulations and enzymatic synthesis via β-1,4-galactosyltransferase-mediated transglycosylation from UDP-Gal as the donor to (GlcNAc)₂-β-pNP as the acceptor. Hydrolysis of the synthesized Gal(GlcNAc)₂-β-pNP and related compounds using hen egg-white lysozyme (HEWL) demonstrated that the substrate was specifically cleaved to Gal(GlcNAc)₂ and p-nitrophenol (pNP). A combination of kinetic studies and docking simulation was further conducted to elucidate the mode of substrate binding. The results demonstrate that Gal(GlcNAc)₂-β-pNP selectively binds to a subsite of lysozyme to liberate the Gal(GlcNAc)₂ and pNP products. The work therefore describes a new colorimetric method for quantifying lysozyme on the basis of the determination of pNP liberated from the substrate.     

Chromosome translocation induced by the insertion of the URA blaster into the major repeat sequence (MRS) in Candida albicans

Electrophoretic karyotype studies have shown that clinical isolates of Candida albicans have extensive chromosome length polymorphisms. Chromosome translocation is one of the causes of karyotypic variation. Chromosome translocation events have been shown to occur very frequently at or near the major repeat sequence (MRS) on chromosomes. The MRS consists of the repeated sequences RB2, RPS and HOK, and the repeated sequences are considered to be the template for recombination. To investigate which element of the MRS is important for chromosome translocation, we constructed three cassettes, each containing a URA blaster and sequences homologous to one of the repeats, for insertion into the MRS region on the chromosomes. The ura3 strain STN22u2, which shows a stable, standard karyotype, was transformed with each construct. Insertion events with each cassette occurred at almost all chromosomes. Insertion into the RB2 repeat, but not into the RPS repeat, was accompanied by chromosome translocation in some transformants: chromosome translocations between chromosomes R and 7 and chromosomes 1 and 7 were found, as well as deletions of 7A and 7C from chromosome 7. We conclude that the insertion at the RB2 region may initiate chromosome translocation in C. albicans.     

Functional analysis of genes encoding putative oxidoreductases in Aspergillus oryzae, which are similar to fungal fructosyl-amino acid oxidase

We found 11 genes (FAO1-11) encoding putative oxidoreductases in the Aspergillus oryzae genome, which are similar to fungal fructosyl-amino acid oxidases. The cDNAs corresponding to the genes were cloned and expressed in Escherichia coli. rFao2 had fructosyl-amino acid oxidase activity, whereas rFao1 did not show any enzyme activity, even though the deduced amino acid sequence of Fao1 is identical to that of one of the fructosyl-amino acid oxidase isozymes from Aspergillus oryzae. rFao7 and rFao8 showed oxidase activity toward sarcosine, L-pipecolate, and L-proline. rFao10 was active toward only sarcosine, of the substrates tested. The functions of the other proteins were also predicted from a phylogenetic analysis.     

Dioxin-like and transthyretin-binding compounds in indoor dusts collected from Japan: average daily dose and possible implications for children

Many researchers are increasingly interested in human exposure to house dust containing household compounds such as polybrominated diphenylethers (PBDEs). Nevertheless, no investigations have addressed the endocrine-disrupting potencies of compounds contained in indoor dust. This study specifically addresses endocrine-disrupting potencies such as dioxin-like activity and human transthyretin (TTR)-binding potencies. Using in vitro bioassays, we investigated these activity levels in indoor dusts. We performed exposure assessments of active compounds that are contained in house dust for subsequent evaluation of house dusts' risks to humans. Dioxin-like and TTR-binding activities in sulfuric acid treatment extracts of house and office dust were investigated using Dioxin-Responsive Chemical-Activated LUciferase gene eXpression assay (DR-CALUX) and TTR-binding assay (in vitro competitive human TTR-binding assay). Dioxin-like activities in indoor dust were 38-1400 pg CALUX-TEQ (2,3,7,8-TCDD equivalent)/g (median 160 pg CALUX-TEQ/g) and TTR-binding potencies were 300-5000 pmol T4EQ (thyroxine (T4) equivalent)/g (median 1000 pmol T4EQ/g), which are higher values than those in other environmental samples, e.g., contaminated sediments. These exposure results suggest that children might be affected by both dioxin-like compounds and TTR-binding compounds via house dust. When the ingestion rate, CALUX-TEQ, and T4EQ for house dust are high, thyroid hormone homeostasis in children may be disrupted.     

Field instrument for simultaneous large dynamic range measurement of atmospheric hydrogen sulfide, methanethiol, and sulfur dioxide

We describe a membrane-based collection/analysis system that differentially monitors H2S and CH3SH, and to which a conductometric SO2 analyzer using the same collector was coupled. A diffusion scrubber (DS) comprised of a Nafion tube collects H2S selectively while a porous polytetrafluoroethylene (pPTFE) DS collects both H2S and CH3SH. Both gases are measured via their ability to react with fluorescein mercuric acetate (FMA) which results in decreased fluorescence. The limited dynamic range of a negative signal procedure was overcome by using dual DS units comprised of short and long scrubbers, placed serially in the liquid flow line. Different DS designs and membrane materials were investigated. H2S, CH3SH, and SO2 from a biogenic point source were continuously measured, and the H2S/CH3SH data compared well with a standard procedure involving Tedlar bag collection, preconcentration and thermal desorption from a Tenax trap, and measurement by gas chromatography/flame photometric detection. Walkaround portability of the instrument and very large dynamic range measurement of H2S and SO2 were demonstrated around the Mt. Aso volcano.     

Nitrogen starvation induces expression of Lg‐FLO1 and flocculation in bottom‐fermenting yeast

When exponentially growing cells of bottom‐fermenting yeast were starved for nitrogen or were grown on proline (a non‐preferred nitrogen source), flocculation was induced. This flocculation was not induced by starvation for either carbon or amino acids. Expression of Lg‐FLO1, which is required for flocculation of bottom‐fermenting yeast, was also found to be induced by starvation for nitrogen. This suggests that the flocculation of bottom‐fermenting yeast is under the control of a nitrogen catabolite repression (NCR)‐like mechanism. Copyright © 2012 John Wiley & Sons, Ltd.     

Sphingomyelinase C from Streptomyces sp. A9107: Unusual primary structure for bacterial sphingomyelinase C

A sphingomyelinase C (SMase) was identified in the culture supernatant of Streptomyces sp. A9107 (S-SMase). Although S-SMase seems to be a typical bacterial SMase, the primary structure of S-SMase was unusual for known bacterial SMase. The gene was functionally overexpressed in the culture medium of recombinant Rhodococcus erythropolis.