Abstract:
The wood adhesive market is very large and problems due to volatile organic compounds and toxic chemicals in many adhesives and their production are significant. In addition, most of the adhesives are derived from depleting petrochemical resources. An environmentally friendly wood adhesive based on renewable resources and produced by microbial fermentation has been explored. Using the shear block test method, a microbially produced polysaccharide has been tested and the effects of wood type, humidity, set time, partial acetylation, and surface wetting agents were determined. Shear strength of the microbial polysaccharide adhesive was compared to that of a commercial wood adhesive and other polysaccharides. Shear strengths of up to 20MPa (3000psi) for bonding maple have been obtained at 53% relative humidity and 22°C. © 2004 Elsevier Ltd. All rights reserved.
Abstract:
Syntheses of the bacterial surfactants 6S,6S-, 9S,9S-, and 9U,9U-flavolipids confirmed the structures proposed for them from spectroscopic analysis of a flavolipid mixture and made pure flavolipids available for the first time. All three synthetic flavolipids and a straight chain analogue were found to be weakly cytotoxic and to inhibit metastatic cancer cell migration, with 9U,9U-flavolipid (the most abundant natural flavolipid) having the most activity. Biosynthetic routes to the branched side-chains of the flavolipids are suggested, and it is proposed that branched chains are employed to hinder biodegradation. © 2010 Elsevier Ltd. All rights reserved.
PMID: 2106288;Abstract:
The reaction of glycogen phosphorylase b and creatine kinase with glutathione disulfide, cystine, and cystamine was compared by direct analysis on electrofocusing gels. This method was useful for individual proteins or for mixtures of the proteins. Millimolar concentrations of glutathione disulfide were required for both proteins and the rate of modification of each protein was similar. The reaction of glutathione disulfide with creatine kinase was inhibited by reduced glutathione (GSH), but the effect on the reaction with phosphorylase was minimal. Cystine and cystamine were required in micromolar amounts to effectively form the disulfide adducts. Both proteins were modified by cystine but cystamine reacted only with phosphorylase. Cystamine (10 μm) was an effective inhibitor of the reaction of phosphorylase b with 2 mm glutathione disulfide. S-thiolation of creatine kinase inactivated the enzyme and a direct assay of the enzyme activity could be used to quantitate S-thiolation of this protein by each of the disulfides. The effect of each disulfide on enzyme activity confirmed the results obtained by gel electrofocusing. Glutathione disulfide and cystine both inactivated the enzyme while cystamine had no effect on the activity. S-thiolation of phosphorylase had no observable effect on any activity parameter, but it effectively prevented binding of phosphorylase to high-molecular-weight glycogen, probably at the glycogen storage site of phosphorylase. The rate of S-thiolation of a mixture of phosphorylase and creatine kinase by thiol-disulfide exchange with glutathione disulfide was compared to the rate of S-thiolation of these proteins by a xanthine oxidase-initiated process (presumably due to protein sulfhydryl activation by reactive oxygen species). The xanthine oxidase-initiated mechanism was somewhat faster than thiol-disulfide exchange with both proteins. It was shown that GSH inhibited S-thiolation of creatine kinase by this mechanism as well as by thiol-disulfide exchange. It is suggested that both mechanisms may play a role in protein S-thiolation in vivo. For proteins that are typified by creatine kinase, the concentration of GSH in the cells may determine whether the S-thiolated form of the protein accumulates. For proteins typified by phosphorylase b, the accumulation of S-thiolated forms may be more independent of GSH. © 1990.
Abstract:
Evaporative deposition from a sessile drop is an appealing way to deposit materials on a surface due to the simplicity of the technique. In this work we deposit aqueous solutions of two types of colloidal particles, namely bacteria and microspheres, on mica. We show that by controlling the extent of initial drop spreading through subtle changes in surface conditioning caused by exposure to the laboratory atmosphere in a laminar flow hood it is possible to systematically vary the particle deposition patterns. On freshly cleaved mica the contact angle of water is 5°. Drops of bacterial and microsphere solutions deposited on freshly cleaved mica spread to cover a large surface area. Drying occurs through pinning and depinning events leaving a series of colloidal particle rings. We found in our laboratory that the contact angle of water on mica exposed to a constant flow of filtered laboratory air in a laminar flow hood gradually increases with time. For drops of both bacterial and microsphere solutions there is a corresponding decrease in the extent of drop spreading with increasing exposure of the mica surface to laboratory air. This results in a profound change in the colloidal particle deposition pattern. Short exposures of minutes to hours are enough to decrease spreading and affect the resulting deposition pattern. For our longest mica surface exposure times (months to 1 year) the contact angle of water reaches values near 20°. Spreading of the bacterial and microsphere drops is substantially decreased. A portion of the colloidal particles are deposited in an outer deposition ring which marks the extent of drop spreading and the remainder of the particles are deposited in the drop interior as a honeycomb or cellular film. The fraction of the drop residue covered with the cellular film increases with particle concentration as well as the length of time the mica is exposed to the laboratory atmosphere. This work shows that evaporative deposition on mica is very sensitive to surface conditioning through atmospheric exposure and also suggests that particle deposition patterns can be tuned by small changes in drop spreading. © 2010 Materials Research Society.
PCR-denaturing gradient gel electrophoresis (PCR-DGGE) is widely used in microbial ecology for the analysis of comparative community structure. However, artifacts generated during PCR-DGGE of mixed template communities impede the application of this technique to quantitative analysis of community diversity. The objective of the current study was to employ an artificial bacterial community to document and analyze artifacts associated with multiband signatures and preferential template amplification and to highlight their impacts on the use of this technique for quantitative diversity analysis. Six bacterial species (three Betaproteobacteria, two Alphaproteobacteria, and one Firmicutes) were amplified individually and in combinations with primers targeting the V7/V8 region of the 16S rRNA gene. Two of the six isolates produced multiband profiles demonstrating that band number does not correlate directly with alpha-diversity. Analysis of the multiple bands from one of these isolates confirmed that both bands had identical sequences which lead to the hypothesis that the multiband pattern resulted from two distinct structural conformations of the same amplicon. In addition, consistent preferential amplification was demonstrated following pairwise amplifications of the six isolates. DGGE and real rime PCR analysis identified primer mismatch and PCR inhibition due to 16S rDNA secondary structure as the most probable causes of preferential amplification patterns. Reproducible DGGE community profiles generated in this study confirm that PCR-DGGE provides an excellent high-throughput tool for comparative community structure analysis, but that method-specific artifacts preclude its use for accurate comparative diversity analysis. (C) 2013 Elsevier B.V. All rights reserved.
