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At least 865 records · Page 48Linked to original sources
PubMed2001

Influence of the solute hydrophobicity on the enantioselective adsorption of beta-blockers on a cellulase protein used as the chiral selector.

Adsorption isotherm data were acquired at different eluent pH values for the enantiomers of several beta-blockers on cellobiohydrolase I on silica gel. They fit well to the biLangmuir model, allowing the determination of the equilibrium constants and the monolayer capacities for chiral and nonselective adsorption. The adsorption of the S-enantiomers (eluted second) is exothermic at low pH, endothermic at high pH, and athermal in a narrow pH range depending on the beta-blocker. This transition pH range is lower for S-alprenolol than for the more hydrophobic S-propranolol, although their endothermic adsorption originates from hydrophobic interactions. This surprising observation is explained by the relative values of the isotherm coefficients. S-Alprenolol seems to have a more pronounced endothermic behavior than S-propranolol because the nonselective interactions of both compounds with the stationary phase are exothermic but their contribution to retention, relative to that of the endothermic chiral interactions, is less important for alprenolol. The order of increasing energy of the chiral interactions is the same as that of hydrophobicity, propranolol>alprenolol>metoprolol.

Adrenergic beta-Antagonists↗
PubMed1997

High level production of a cellulase-free xylanase in glucose-limited fed batch cultures of a thermophilic Bacillus strain.

Bacillus sp. strain XE and its mutant derivative strain D3 produce a thermostable xylanase which is suitable for enzymatic bleaching of kraft pulp. Xylanase synthesis was shown to be induced by the soluble products of xylan hydrolysis (xylooligosaccharide) and equally, catabolically-repressed when these oligosaccharides accumulate in the medium. An optimal balance between these two antagonistic effects was obtained in a carbon-limited, fed-batch culture with continuous xylooligosaccharide feeding. To reduce substrate cost, the xylooligosaccharide could be 90% substituted by glucose without reduction of the xylanase production rate. Xylanase production ceased when the activity reached approximately 380 U ml-1 due to an amino acid shortage. A continuous supply of exogenous amino acids allowed the production to continue to more than 1000 U ml-1.

Amino Acids↗
PubMed2003

Purification and characterization of a novel cellulase-free xylanase from Acrophialophora nainiana.

A beta-xylanase (XynIII) of Acrophialophora nainiana was purified to homogeneity from the culture supernatant by ultrafiltration and a combination of ion exchange and gel filtration chromatographic methods. It was optimally active at 55 degrees C and pH 6.5. XynIII had molecular masses of 27.5 and 54 kDa, as estimated by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, respectively. The purified enzyme hydrolyzed preferentially xylan as the substrate. The half-lives of XynIII at 50 and 60 degrees C were 96 and 1 h, respectively. It was activated by L-tryptophan, dithiothreitol, 5,5-dithio-bis(2-nitrobenzoic acid, L-cysteine and beta-mercaptoethanol and strongly inhibited by N-bromosuccinimide. The presence of carbohydrate was detected in the pure XynIII.

Cellulase↗
PubMed1996

Experimental and theoretical study of the adsorption behavior and mass transfer kinetics of propranolol enantiomers on cellulase protein as the selector.

The thermodynamics and mass transfer kinetics of the retention of the R and S enantiomers of propranolol were investigated on a system comprising an acetic acid buffer solution as the mobile phase and the protein cellobiohydrolase I immobilized on silica as the stationary phase. The bi-Langmuir isotherm model fitted best to each set of single-component isotherm data. The monolayer capacity of the nonchiral type of adsorption sites was 22.9 mM. For the chiral type of sites, it was 0.24 mM for the R enantiomer and 0.64 mM for the S enantiomer. Peak tailing was observed, even at very low concentrations allowing operation of the low-capacity chiral sites under linear conditions. This tailing can be explained on the basis of heterogeneous mass transfer kinetics. At higher concentrations, which are often used in analytical applications, the isotherms on the chiral sites no longer have a linear behavior, and peak tailing is consequently more pronounced. Under those conditions, peak tailing originates from the combined effect of heterogeneous thermodynamics and heterogeneous mass transfer kinetics. These complex phenomena are explained and modeled using the transport-dispersive model with a solid film linear driving force model modified to account for heterogeneous mass transfer kinetics. The rate coefficient of the mass transfer kinetics was found to be concentration dependent.

Adsorption↗
PubMed2000

Retention mechanism of beta-blockers on an immobilized cellulase. Relative importance of the hydrophobic and ionic contributions to their enantioselective and nonselective interactions.

The adsorption isotherms of the enantiomers of three beta-blockers, metoprolol, alprenolol, and propranolol, were measured on cellobiohydrolase I (CBH I) immobilized on silicagel, in the concentration range between 0.25 microM and 1.7 mM, at pH = 5.0, 5.5, and 6.0. In agreement with previous results, these data are accounted for by a two-sites physical model and fit closely to a Bilangmuir equation. The saturation capacities and the binding constants were determined for each enantiomer on the chiral and the nonchiral sites. The chiral sites are shown to be strongly ionic, in contrast to the nonchiral ones, which are mainly hydrophobic. However, the chiral binding of (S)-propranolol is endothermic, with a high adsorption entropy, in contrast to the chiral interactions of (R)-propranolol and to the nonchiral interactions, which are all exothermic. This indicates that hydrophobic interactions also play a role in the chiral binding. The dependence of the adsorption parameters on the hydrophobicity of the solute is discussed and interpreted in terms of the retention mechanism. The results are compared with the structure of the protein, recently elucidated by X-ray crystallography.

Adrenergic beta-Antagonists↗
PubMed1996

Folding and stability of endoglucanase III, a single-domain cellulase from Trichoderma reesei.

The reversible folding of an endoglucanase (EGIII) from the filamentous fungus Trichoderma reesei was investigated by activity, tryptophan fluorescence, and peptide CD measurements. Equilibrium stability was determined by urea denaturation at various pH and temperature values. Unfolding and refolding rates were measured over a range of urea concentrations. The data from the equilibrium and kinetic studies fit a simple two-state model, except at lower urea concentrations, where the folding kinetics indicate a transient intermediate. Unfolding is very slow, with a half-life of about 2 h in 8 M urea at pH 5.5 and 25 degrees C. Comparison of the urea dependence of the folding kinetics and equilibrium indicates the protein undergoes 93% of its total change in solvent exposure on going from the unfolded state to the transition state. Thus, the transition state is quite compact. The presence of dithiothreitol destabilized the protein by 7 kcal/mol, indicating the presence of an unusually strong disulfide linkage between the two cysteines in the molecule. Protein stability is dramatically reduced at alkaline pH values; this can be attributed to a titratable shift (pKa = 7.8) in the slope of the urea dependence of unfolding.

Bacterial Proteins↗