Saturated liquid viscosities and densities of environmentally acceptable hydrochlorofluorocarbons (HCFCs)

Measurements of saturated liquid viscosities and densities were performed on environmentally acceptable hydrochlorofluorocarbons (HCFCs), CHb>3b>CClb>2b>F (HCFC-141b), CHb>3b>CClFb>2b> (HCFC-142b; only for viscosity), CFb>3b>CFb>2b>CHClb>2b> (HCFC-225ca), and CClFb>2b>CFb>2b>CHClF (HCFC-225cb), using a capillary viscometer and a glass pycnometer in the temperature range from 273 to 353 K. The uncertainty in the measurement of viscosity is estimated to be 5% based on the comparison of the present data with those in the literature for HCFC-141b. An equation is given to represent our saturated liquid viscosity data as a function of temperature.     

Low-dimensional modelling of dynamics via computer algebra

I describe a method, particularly suitable to implementation by computer algebra, for the derivation of low-dimensional models of dynamical systems. The method is systematic and is based upon centre manifold theory. Computer code for the algorithm is relatively simple, robust and flexible. The method is applied to two examples: one a straightforward pitchwork bifurcation, and one being the dynamics of thin fluid films.     

Immobilization of an endopectinlyase on γ-alumina: Study of factors influencing the biocatalytic matrix stability

Endopectinlyase (EC 4.2.2.10) from Aspergillus japonicus was immobilized on to γ-alumina. Adsorption performed at pH 5·0 and a subsequent cross-linking phase using 0·1% glutaraldehyde were the chosen immobilization conditions. The comparison between the main biochemical parameters of the immobilized and free form of the enzyme showed that the immobilization procedure used did not affect the enzyme biochemical properties. The interactions between the carrier and the enzyme are essentially secondary bonding. In fact they depend on the pH and on the presence of phosphate ions in the medium. A tentative chemical model of the biocatalytic matrix thus obtained is proposed.     

Brandschutz; subjektiv-?ffentliche Nachbarrechte

Nachbarn kommt kein Mitspracherecht dahingehend zu, dass die Zufahrt für Einsatzfahrzeuge der Feuerwehr gew?hrleistet sein müsste.     

The identification of highly chlorinated ethers and diethers in river sediment near an epichlorohydrin plant

In harbour sediment samples taken near an epichlorohydrin production plant, a series of highly chlorinated ethers and diethers were detected viz. three isomeric bis(dichloropropyl)ethers, several structurally closely related ethers with 9 carbon atoms (Cb>9b> ethers), a number of Cb>12b> ethers and diethers, and finally several Cb>15b> ethers. The formation of this new class of ether compounds can be explained on the basis of the chemistry of the addition of HOCl to allylchloride. After initial addition of Cl⁻, a reactive intermediate is formed which may react with the product dichloropropanol, to give the Cb>6b> ethers, or may polymerize with the starting compound allylchloride followed by reaction with the product, to give the Cb>9b>, Cb>12b> and Cb>15b> ethers.     

The influence of the ion content of whey on the pH-activity profile of the β-galactosidase from Aspergillus oryzae

The pH-dependence of the reaction kinetics of lactase (β-galactosidase) from Aspergillus oryzae in different reaction media is presented in terms of a two-parameter model. The lactase from A. oryzae seems to have replaced the A. niger lactase on the market owing to a better activity/price ratio and may be utilised for lactose hydrolysis in acid as well as in neutral milk products. Its pH optimum is around pH 4.5. However, in the neutral pH-range its activity depended strongly on the salt content of the substrate solution. For example, its activity in whey (pH 6.5) fell to only 30% of its expected activity in a pure lactose solution at the same pH. The whey effect was the same for both soluble and immobilised lactase. The two parameter kinetic model, which included a term for competitive product inhibition gave excellent agreement with experimental data, and may thus be useful for the prediction of reactor performance with this enzyme.     

β-hydroxyacyl-coa-dehydrogenase (HADH) activity of unfrozen and frozen—thawed frog (Rana esculenta) legs

The β-hydroxyacyl-CoA-dehydrogenase (HADH) activity of unfrozen and thawed frog legs was investigated. The enzyme was extracted by either immersing frog legs in phosphate buffer 0.1 M, pH 6.0 at 25°C for 15 min or pressing them between trichinoscopy glasses. The enzyme activity was assayed using acetoacetyl-CoA as substrate and measured spectrophotometrically at 340 nm. It was possible by both extraction methods to distinguish between thawed and unfrozen samples although when the juice was obtained by pressing the HADH activity of the dilution was ～ 1.5 times higher than that obtained by immersion. The HADH activity was significantly higher (P≤0·001) in frozen-thawed frogs than in unfrozen legs because during freezing there is a release of HADH. No significative differences were found in the HADH activity in samples frozen in the temperature range -10 to -196°C. HADH activity was not affected by the storage time in crushed ice up to 6 days.     

Yeast exo-β-glucanases can be used as efficient and readily detectable reporter genes in Saccharomyces cerevisiae

Yeast exo-1,3-β-glucanases are secretable proteins whose function is basically trophic and may also be involved in cell wall glucan hydrolytic processes. Since fluorescein di(β-D -glucopyranoside) is a fluorogenic substrate detectable and quantifiable by flow cytometry, it was used for testing the ability of the EXG1 gene product of Saccharomyces cerevisiae and its homologous gene in Candida albicans to function as reporter genes. These open reading frames were coupled to different promoters in multicopy plasmids, and exoglucanase activity quantified at flow cytometry. Exoglucanases were found to be useful tools for the study of promoter regions in S. cerevisiae. This technique has the advantage over other reporter gene systems—such as β-galactosidase fusions—that it does not require permeabilization of yeast cells and therefore it allows the recovery of viable cells—by sorting—after flow cytometry analysis.     

Purification and renaturation of recombinant human lymphotoxin (tumour necrosis factor beta) expressed in Escherichia coli as inclusion bodies

High level expression of recombinant human tumour necrosis factor β (rh TNF-β) in Escherichia coli results in the formation of two portions of protein, namely soluble active protein and insoluble protein which is inactive and aggregates in the form of inclusion bodies (IBs). In this study, a procedure for purification and renaturation of rh TNF-β from inclusion bodies has been designed and verified experimentally with a product purity of more than 90% and a recovery of about 30%. The procedure includes washing of IBs with specific wash buffer (Triton X-100/EDTA/lysozyme/PMSF), their solubilization with 8 mol dm^?3 alkaline urea, purification with ion-exchange columns, refolding with renaturation buffer and finally concentration and desalination with an ultrafiltration membrane. The characteristics of the renatured protein were identical with those of purified protein from the soluble fraction as demonstrated by (1) SDS-PAGE, (2) cytotoxic activity on mouse L929 cells, (3) N-terminal amino acid sequence, and (4) gel filtration chromatography.     

Liquid–liquid extraction of a recombinant protein with reverse micelles

Recombinant cytochrome bb>5b> was extracted into the reversed micelle phase of an anionic surfactant (AOT) in octane and back-extracted to a final aqueous phase. The extraction of the protein was controlled by an electrostatic mechanism, since it was dependent on the global charge of the protein. This was directly demonstrated by experiments with native and mutant cytochromes obtained by site directed mutagenesis. The back-extraction of cytochrome bb>5b> to a fresh aqueous phase was decreased by factors that reduced the size of the water pool of the organic phase, such as high salt concentrations (1–2 mol dm^?3 NaCl) and low temperatures (4°C), probably because of an increase in a favourable interaction of this protein with the surfactant at closer distances.