Free-solution, label-free molecular interactions were investigated with back-scattering interferometry in a simple optical train composed of a helium-neon laser, a microfluidic channel, and a position sensor. Molecular binding interactions between proteins, ions and protein, and small molecules and protein, were determined with high dynamic range dissociation constants (K d spanning six decades) and unmatched sensitivity (picomolar K d 's and detection limits of 10,000s of molecules). With this technique, equilibrium dissociation constants were quantified for protein A and immunoglobulin G, interleukin-2 with its monoclonal antibody, and calmodulin with calcium ion Ca 2+ , a small molecule inhibitor, the protein calcineurin, and the M13 peptide. The high sensitivity of back-scattering interferometry and small volumes of microfluidics allowed the entire calmodulin assay to be performed with 200 picomoles of solute.

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A fast pyrolysis study on lignin and macroalgae (nonconventional biomass) and wood and straw (conventional biomass) were carried out in a pyrolysis centrifugal reactor at pyrolysis temperature of 550 °C. The product distributions and energy recoveries were measured and compared among these biomasses. The fast pyrolysis of macroalgae showed a promising result with a bio-oil yield of 65 wt % dry ash free basis (daf) and 76% energy recovery in the bio-oil while the lignin fast pyrolysis provides a bio-oil yield of 47 wt % daf and energy recovery in bio-oil of 45%. The physiochemical properties of the bio-oils were characterized with respect to higher heating value (HHV), molecular mass distribution, viscosity, pH, density, thermal behaviors, elemental concentrations, phase separation, and aging. The lignin and macroalgae oil properties were different compared to those of the wood and straw oils with respect to carbon and oxygen contents, HHV, thermal behaviors, and mean molecular weight. The HHV of wood, straw, lignin, and algae oils were 24.0, 23.7, 29.7, and 25.7 MJ/kg db, respectively. The distributions of metals, Cl and S in char and bio-oil were investigated for the biomasses. Almost all the metals (Al, Ca, Fe, K, Mg, Na, P, and Si) were contained in the chars at the pyrolysis temperature of 550 °C. The char properties were characterized, and their potential applications are discussed.

Hydrolysis of arabinoxylan is an important prerequisite for improved utilization of wheat hemicellulose in the ethanol fermentation industry. This study investigates the individual and combined efficiencies of three commercial, cellulytic and hemicellulytic enzyme preparations, Celluclast 1.5 L, Ultraflo L, and Viscozyme L, in catalyzing the liberation of arabinose and xylose from water-soluble wheat arabinoxylan. Ultraflo L was the best enzyme preparation for releasing arabinose, liberating 53 wt% of the theoretical maximum after 48 h of reaction (10 wt% enzyme/substrate ratio, 40 degrees C, pH 6). Celluclast 1.5 L was superior to the other enzyme preparations in releasing xylose, liberating 26 wt% of the theoretical maximum after 48 h of reaction (10 wt% enzyme/substrate ratio, 50 degrees C, pH 5). The 50:50 mixtures of the enzyme preparations showed no synergistic cooperation in arabinose release, but a synergistic interaction in xylose release was found between Ultraflo L and Celluclast 1.5 L. On the basis of high-performance anion exchange chromatography (HPAEC) analysis of the hydrolysates after enzymatic reaction, we propose that the observed synergism between Celluclast 1.5 L and Ultraflo L is the result of positive interaction between alpha-L-arabinofuranosidase and endo-1,4-beta-xylanase activities present in Ultraflo L that released arabinose, xylobiose and xylotriose, and beta-xylosidase activities in Celluclast 1.5 L, capable of catalyzing the hydrolysis of xylobiose and xylotriose to xylose.

Fast pyrolysis may be used for sewage sludge treatment with the advantages of a significant reduction of solid waste volume and production of a bio-oil that can be used as fuel. A study of the influence of the reaction temperature on sewage sludge pyrolysis has been carried out using a pyrolysis centrifugel reactor (PCR) at 475, 525, 575, and 625 °C. Maxima of both organic oil yield of 41 wt % on a dry ash free feedstock basis (daf) and a sludge oil energy recovery of 50% were obtained at 575 °C. The water-insoluble fraction, molecular-weight distribution, higher heating value (HHV), and thermal behaviors of sludge oils were found to be considerably influenced by the applied pyrolysis temperatures. The sludge oil properties obtained at the optimal temperature of 575 °C were a HHV of 25.5 MJ/kg, a water-insoluble fraction of 18.7 wt %, a viscosity of 43.6 mPa s at 40 °C, a mean molecular weight of 392 g/mol, and metal concentrations lower than 0.14 wt % on a dry basis (db). Less optimal oil properties with respect to industrial applications were observed for oil samples obtained at 475 and 625 °C. Char properties of the 575 °C sample were an ash content of 81 wt % and a HHV of 6.1 MJ/kg db. A total of 95% of the sewage sludge phosphorus content was recovered in the char. The solid waste amount (char compared to sludge) was reduced to 52% on a bulk volume basis at the pyrolysis temperature of 575 °C.

A novel alpha-L-arabinofuranosidase (alpha-AraF) belonging to glycoside hydrolase (GH) family 43 was cloned from Humicola insolens and expressed in Aspergillus oryzae. (1)H-NMR analysis revealed that the novel GH43 enzyme selectively hydrolysed (1-->3)-alpha-L-arabinofuranosyl residues of doubly substituted xylopyranosyl residues in arabinoxylan and in arabinoxylan-derived oligosaccharides. The optimal activity of the cloned enzyme was at pH 6.7 and 53 degrees C. Two other novel alpha-L-arabinofuranosidases (alpha-AraFs), both belonging to GH family 51, were cloned from H. insolens and from the white-rot basidiomycete Meripilus giganteus. Both GH51 enzymes catalysed removal of (1-->2) and (1-->3)-alpha-L-arabinofuranosyl residues from singly substituted xylopyranosyls in arabinoxylan; the highest arabinose yields were obtained with the M. giganteus enzyme. Combinations (50:50) of the GH43 alpha-AraF from H. insolens and the GH51 alpha-AraFs from either M. giganteus or H. insolens resulted in a synergistic increase in arabinose release from water-soluble wheat arabinoxylan in extended reactions at pH 6 and 40 degrees C. This synergistic interaction between GH43 and GH51 alpha-AraFs was also evident when a GH43 alpha-AraF from a Bifidobacterium sp. was supplemented in combination with either of the GH51 enzymes. The synergistic effect is presumed to be a result of the GH51 alpha-AraFs being able to catalyse the removal of single-sitting (1-->2)-alpha-L- arabinofuranosyls that resulted after the GH43 enzyme had catalysed the removal of (1-->3)-alpha-L-arabinofuranosyl residues on doubly substituted xylopyranosyls in the wheat arabinoxylan.

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