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There is current interest in replacing petroleum-based additives in consumer paper products with abundantly available, renewable and sustainable biopolymers such as lignin-containing cellulose nanofibers (LCNFs) and cottonseed protein. This research characterized the performance of cottonseed protein isolate with/without LCNFs to increase the dry strength of filter paper. The application of 10% protein solution with 2% LCNFs as an additive improved the elongation at break, tensile strength and modulus of treated paper products compared to the improved performance of cottonseed protein alone. Improvements in tensile modulus and tensile strength were greatest for samples containing larger amounts of lignin and a greater degree of polymerization than for those with less lignin from the same biomass sources. [ABSTRACT FROM AUTHOR]

A simple method is described for the patterned deposition of Teflon on paper to create an integrated platform for parallel organic synthesis and cell-based assays. Solvent-repelling barriers made of Teflon-impregnated paper confine organic solvents to specific zones of the patterned array and allow for 96 parallel flow-through syntheses on paper. The confinement and flow-through mixing significantly improves the peptide yield and simplifies the automation of this synthesis. The synthesis of 100 peptides ranging from 7 to 14 amino acids in length gave over 60 % purity for the majority of the peptides (>95 % yield per coupling/deprotection cycle). The resulting peptide arrays were used in cell-based screening to identify 14 potent bioactive peptides that support the adhesion or proliferation of breast cancer cells in a 3D environment. In the future, this technology could be used for the screening of more complex phenotypic responses, such as cell migration or differentiation. [ABSTRACT FROM AUTHOR]

Active cellulose-based packaging materials were prepared by binding lactoferrin to paper modified with anionic polyelectrolytes. About 63% of the protein added in the slurry was present in the finished paper, corresponding to about 0.28 mg protein per cm2 of the glassine paper produced. The efficacy of the activated materials was assessed by microbiological trials, employing targets bacteria considered as spoilage and/or pathogens in food products. Lactoferrin-activated paper evidenced its efficacy against growing cells of E. coli and L. innocua, with a maximum of 0.3 and 1.3 log cycles reduction of the final population, respectively. These results can be considered a promising starting point and will be the focus of further research, aimed at developing innovative cellulose-based active food packaging. [ABSTRACT FROM AUTHOR]

Paper has been proposed as an inexpensive and versatile carrier for microfluidics devices with abilities well beyond simple capillary action for pregnancy tests and the like. Unlike standard microfluidics devices, extracting a fluid from the paper is a challenge and a drawback to its broader use. Here, we extract fluid from narrow paper strips using surface acoustic wave (SAW) irradiation that subsequently atomizes the extracted fluid into a monodisperse aerosol for use in mass spectroscopy, medical diagnostics, and drug delivery applications. Two protein molecules, ovalbumin and bovine serum albumin (BSA), have been preserved in paper and then extracted using atomized mist through SAW excitation; protein electrophoresis shows there is less than 1% degradation of either protein molecule in this process. Finally, a solution of live yeast cells was infused into paper, which was subsequently dried for preservation then remoistened to extract the cells viaSAW atomization, yielding live cells at the completion of the process. The successful preservation and extraction of fluids, proteins and yeast cells significantly expands the usefulness of paper in microfluidics. [ABSTRACT FROM AUTHOR]

When yeast cells enter into quiescence in response to nutrient limitation, the adenine deaminase Aah1p is specifically degraded via a process requiring the F-box protein Saf1p and components of the Skp1-Cullin-F-box complex. In this paper, we show that Saf1p interacts with both Aah1p and Skp1p. Interaction with Skp1p, but not with Aah1p, requires the F-box domain of Saf1p. Based on deletion and point mutations, we further demonstrate that the F-box domain of Saf1p is critical for degradation of Aah1p. We also establish that overexpression of Saf1p in proliferating cells is sufficient to trigger the degradation of Aah1p. Using this property and a two-dimensional protein gel approach, we found that Saf1p has a small number of direct targets. Finally, we isolated and characterized several point mutations in Aah1p, which increase its stability during quiescence. The majority of the mutated residues are located in two distinct exposed regions in the Aah1p three-dimensional model structure. Two hybrid experiments strongly suggest that these domains are directly involved in interaction with Saf1p. Importantly, we obtained a mutation in Aah1p that does not affect the protein interaction with Saf1p but abolishes Aah1p degradation. Because this mutated residue is an exposed lysine in the Aah1p three-dimensional model, we propose that it is likely to be a major ubiquitylation site. All together, our data strongly argue for Saf1p being a bona fide Skp1-Cullin-F-box subunit. [ABSTRACT FROM AUTHOR]

Abstract: Conducting polymer–fibre composites with polypyrrole cellulose (paper) and protein (wool) fibres have been produced by polymerizing pyrrole with ferric chloride as the oxidant around separated individual cellulose (wood) fibres from bleached Pinus radiata Kraft pulp, and merino wool fibres respectively to generate new composite materials that retain the inherent properties of the polymer and individual fibres. For the polypyrrole–cellulose composite, the polypyrrole consisted of spheres of about 100nm in size fused together to form a continuous coating that fully encapsulates the cellulose fibre and associated finer fibrils. For the polypyrrole–wool composite the polypyrrole formed a similar coating of about 200nm spheres. Electrical conductivities of the composites were substantially increased over those of the precursor fibres. [Copyright &y& Elsevier]

We studied the aging behaviour of gelatin used to size paper. Thus far, research on the aging of paper has largely ignored the sizing agent. Degradation of the protein was characterised and the impact of paper components, such as cellulose, and aluminium potassium sulphate was evaluated. Whatman No. 1 filter papers sized with two types of gelatins (A and B) were prepared as model samples. Commercially sized modern papers (Arches) were also studied in order to compare laboratory samples with real artist papers. Both types of papers were artificially aged (80 °C, 50% relative humidity for 35 and 94 days). Historic papers were included in the study in order to compare artificially aged with naturally aged gelatin. The aqueous extracts from the papers were characterised by aqueous size-exclusion chromatography (SEC) using four PL-Aquagel-OH columns and UV photodiode array detection at 220, 254 and 280 nm. Results showed that gelatin undergoes hydrolysis upon aging, type A gelatin showing a faster degradation rate than type B. The result was an increase in the lower-molar-mass fractions, under 50 000 g mol−1, and especially in a characteristic fraction with a peak molecular mass (Mp) of 14 000 g mol−1. A significant decrease in the extraction yields of α-, β- and γ-chains occurred after aging. This was attributed to crosslinking, leading to the formation of less-soluble polypeptides with very high molar mass (>800 000 g mol−1). Less than 10% alum had no impact on the degradation rate; higher alum contents accelerated hydrolysis reactions. [Copyright &y& Elsevier]