Biomedical subjects

Artur Cavaco-Paulo

Publications and source records attributed to Artur Cavaco-Paulo.

15 recordsLinked to original sources

PubMed2007

Using a nitrilase for the surface modification of acrylic fibres.

The surface of an acrylic fibre was modified with a commercial nitrilase (EC 3.5.5.1). The effect of fibre solvents and polyols on nitrilase catalysis efficiency and stability was investigated. The nitrilase action on the acrylic fabric was improved by the combined addition of 1 M sorbitol and 4% N, N-dimethylacetamide. The colour levels for samples treated with nitrilase increased 156% comparing to the control samples. When the additives were introduced in the treatment media, the colour levels increased 199%. The enzymatic conversion of nitrile groups into the corresponding carboxylic groups, on the fibre surface, was followed by the release of ammonia and polyacrylic acid. A surface erosion phenomenon took place and determined the "oscillatory" behaviour of the amount of dye uptake with time of treatment. These results showed that the outcome of the application of the nitrilase for the acrylic treatment is intimately dependent on reaction media parameters, such as time, enzyme activity and formulation.

Acetamides↗

PubMed2006

Stability and decolourization ability of Trametes villosa laccase in liquid ultrasonic fields.

We report in this study that the sonication of laccase from Trametes villosa and bovine serum albumin promotes the formation of protein aggregates with high molecular weight. The formation of aggregates leads to the deactivation of the enzyme, fact that was confirmed by the analysis of the enzyme stability (half-life time) upon ultrasound treatment. This inactivation was mainly caused by the radicals formed by the cavitation phenomenon. It was verified that the addition of polyvinyl alcohol to laccase had a protecting effect against enzyme inactivation. The performance of laccase in the decolourization of indigo carmine was studied. It was observed that the best results were attained when the dye solution was treated with ultrasound and enzyme stabilized with polyvinyl alcohol, where more than 65% of decolourization was achieved. This value is remarkably higher than that attained for the enzyme alone, which was only able to decolourize 20% of the dye solution within 1h of treatment. These results have important implications for the exploitation of sonication in textile industry, where the pollution caused by the release of dyes into effluents is one of the major concerns.

Basidiomycota↗

PubMed2006

Combined ultrasound-laccase assisted bleaching of cotton.

This study evaluates the potential of using ultrasound to enhance the bleaching efficiency of laccase enzyme on cotton fabrics. Ultrasound of low intensity (7W) and relatively short reaction time (30 min) seems to act in a synergistic way with the enzyme in the oxidation/removal of the natural colouring matter of cotton. The increased bleaching effect could be attributed to improved diffusion of the enzyme from the liquid phase to the fibres surface and throughout the textile structure. On the other hand inactivation of the laccase occurred increasing the intensity of the ultrasound. However, at the ultrasound power applied in the bleaching experiments the loss of enzyme activity was not significant enough to justify the use stabilizer such as polyvinyl alcohol. Furthermore, the polyvinyl alcohol appears to be a substrate for the laccase.

Journal Article↗

PubMed2006

Staining of wool using the reaction products of ABTS oxidation by laccase: synergetic effects of ultrasound and cyclic voltammetry.

The effects of ultrasound on 2,2'-Azinobis(3-ethylbenzothiazoline-6-sulfonate) enzymatic oxidation by laccase (Trametes villosa) has been studied by means of cyclic voltammetry. The reaction was allowed to proceed in the presence of a piece of wool and the coloration depth of the wool fabric was measured by means of K/S. It was observed that cyclic voltammetry is influenced the dyeing process and higher K/S values were obtained when the cyclic voltammetry was combined with the ultrasonic irradiation. Moreover, the K/S value is the sum of the values obtained when the wool staining is done in just the presence of cyclic voltammetry or in just the presence of ultrasound. The results obtained on the indigo carmine decolourization gives information on the importance of controlling the amount of ABTS(+) formed during the ultrasonication process.

Animals↗

PubMed2006

Detergent formulations for wool domestic washings containing immobilized enzymes.

The stability of immobilized and native Esperase, a commercial serine protease, was studied by incubating the enzymes in four formulations containing the same amount of anionic and non-ionic surfactants. The results show that the activity of the immobilized enzyme is not affected by the presence of detergents while the native enzyme lost 50% of activity after 20 min of incubation in these four formulations. The washing performance of the detergents prepared with the immobilized Esperase was studied on cotton and wool fabric samples stained with human blood and egg yolk, using as control the detergent containing native Esperase. The best stain removal for cotton samples stained with human blood was achieved using the detergent with immobilized Esperase. Several physical tests confirmed that wool keratin was not degraded by the immobilized Esperase, validating the ability to use formulated detergents containing this immobilized enzyme for safe wool domestic washing.

Animals↗

PubMed2006

New model substrates for enzymes hydrolysing polyethyleneterephthalate and polyamide fibres.

Recently the potential of enzymes for surface hydrophilisation and/or functionalisation of polyethyleneterephthalate (PET) and polyamide (PA) has been discovered. However, there was no correlation between enzyme class/activity (e.g. esterase, lipase, cutinase) and surface hydrolysis of these polymers and consequently no simple assay to estimate this capability. Enzymes active on the model substrates bis (benzoyloxyethyl) terephthalate and adipic acid bishexyl-amide, were also capable of increasing the hydrophilicity of PET and PA. When dosed at the identical activity on 4-nitrophenyl butyrate, only enzymes from Thermobifida fusca, Aspergillus sp., Beauveria sp. and commercial enzymes (TEXAZYME PES sp5 and Lipase PS) increased the hydrophilicity of PET fibres while other esterases and lipases did not show any effect. Activity on PET correlated with the activity on the model substrate. Hydrophilicity of fibres was greatly improved based on increases in rising height of up to 4.3 cm and the relative decrease of water absorption time between control and sample of the water was up to 76%. Similarly, enzymes increasing the hydrophilicity of PA fibres such as from Nocardia sp., Beauveria sp. and F. solani hydrolysed the model substrate; however, there was no common enzyme activity (e.g. protease, esterase, amidase) which could be attributed to all these enzymes.

Actinomycetales↗

PubMed2005

Degradation of azo dyes by Trametes villosa laccase over long periods of oxidative conditions.

Trametes villosa laccase was used for direct azo dye degradation, and the reaction products that accumulated after 72 h of incubation were analyzed. Liquid chromatography-mass spectrometry (LC-MS) analysis showed the formation of phenolic compounds during the dye oxidation process as well as a large amount of polymerized products that retain azo group integrity. The amino-phenol reactions were also investigated by 13C-nuclear magnetic resonance and LC-MS analysis, and the polymerization character of laccase was shown. This study highlights the fact that laccases polymerize the reaction products obtained during long-term batch decolorization processes with azo dyes. These polymerized products provide unacceptable color levels in effluents, limiting the application of laccases as bioremediation agents.

Aminophenols↗

PubMed2004

A new alkali-thermostable azoreductase from Bacillus sp. strain SF.

A screening for dye-decolorizing alkali-thermophilic microorganisms resulted in a Bacillus sp. strain isolated out of the wastewater drain of a textile finishing company. An NADH-dependent azoreductase of this strain, Bacillus sp. strain SF, was found to be responsible for the decolorization of azo dyes. This enzyme was purified by a combination of ammonium sulfate precipitation and anion-exchange and affinity chromatography and had a molecular mass of 61.6 kDa and an isoelectric point at pH 5.3. The pH optimum of the azoreductase depended on the substrate and was within the range of pHs 8 to 9, while the temperature maximum was reached at 80 degrees C. Decolorization only took place in the absence of oxygen and was enhanced by FAD, which was not consumed during the reaction. A 26% similarity of this azoreductase to chaperonin Cpn60 from a Bacillus sp. was found by peptide mass mapping experiments. Substrate specificities of the azoreductase were studied by using synthesized model substrates based on di-sodium-(R)-benzyl-azo-2,7-dihydroxy-3,6-disulfonyl-naphthaline. Those dyes with NO2 substituents, especially in the ortho position, were degraded fastest, while analogues with a methyl substitution showed the lowest degradation rates.

Azo Compounds↗

PubMed2003

Immobilized laccase for decolourization of Reactive Black 5 dyeing effluent.

Reactive Black 5 industrial dyeing effluent was decolourized by free and immobilized laccase. The stability of the enzyme (194 h free and 79 h immobilized) depended on the dyeing liquor composition and the chemical structure of the dye. In the decolourization experiments with immobilized laccase, two phenomenons were observed--decolourization due to adsorption on the support (79%) and dye degradation due to the enzyme action (4%). Dyeing in the enzymatically recycled effluent provided consistency of the colour with both bright and dark dyes.

Biodegradation, Environmental↗

PubMed2003

Effect of some process parameters in enzymatic dyeing of wool.

This article reports on the dyeing of wool using an enzymatic system comprising laccase; dye precursor, 2,5-diaminobenzenesulfonic acid; and dye modifiers, catechol and resorcinol. Enzymatic dyeing was performed as a batchwise process at the temperature and pH of maximum enzyme activity. The effects of the process variables reaction time, enzyme, and modifier concentration on fabric color were studied, according to an appropriate experimental design. Different hues and depths of shades could be achieved by varying the concentration of the modifiers and the time of laccase treatment. The duration of the enzymatic reaction appeared to be the most important factor in the dyeing process. Thus, the dyeing process, performed at low temperature and mild pH, was advantageous in terms of reduced enzyme and chemical dosage.

Analysis of Variance↗

PubMed2002

Hydrogen peroxide generation with immobilized glucose oxidase for textile bleaching.

Glucose oxidase was covalently immobilized on commercially available alumina and glass supports, with a high level of protein recovery. The operational stability of the alumina carrier was an advantage over the glass support, though the rate of generation of hydrogen peroxide in the case of the latter was higher. The immobilization technique provided repeated application of the enzyme even in low concentration, and the hydrogen peroxide generated in the enzymatic reaction was successively used for textile bleaching.

Aluminum Oxide↗

PubMed2002

Voltammetric monitoring of laccase-catalysed mediated reactions.

Six different compounds capable of mediating laccase-catalysed reactions have been tested by cyclic voltammetry. They exhibited quasi-reversible electrodic behaviour with formal redox potentials ranging from 150 to 800 mV (E(0)' vs. SCE). The immersion of a laccase-coated glassy carbon electrode (GCE) in mediator solutions generated large cathodic catalytic currents easily recorded by cyclic voltammetry at low-potential scan rates. This current showed two well-defined pH profiles, which correlated with the variation of the mediator redox potentials at the pH range tested. The relevant effect of temperature on the activity of laccase has been assessed here. Likewise, it was shown that the current record varied with the substrate concentration. This trend fitted Michaelis-Menten kinetics, which allowed us to give an estimation of the affinity of the fungal laccase for the different mediators.

Basidiomycota↗

PubMed2002

Possibilities for recycling cellulases after use in cotton processing: part II: Separation of cellulases from reaction products and released dyestuffs by ultrafiltration.

The adsorption and activity of a total cellulase (Trichoderma reesei) was measured and compared on undyed and dyed cotton fabrics. Recovery of enzymes from the reaction mixture and by desorption from the cotton substrate was evaluated. About 80% of the initial protein could be recovered. The removal of released products (soluble reducing sugars and dyes) from the treatment liquor and subsequent concentration of cellulase proteins was performed using an ultrafiltration membrane. Strong protein-dye interactions made it impossible to separate efficiently the dyes from the enzyme-containing treatment liquors. The use of surfactants did not enhance cellulase desorption from cotton fabric. Although anionic surfactants have a deactivating effect on cellulases, this effect seems to be reversible, since after ultrafiltration the cellulase activity was similar to that of enzymes desorbed with buffer only. Humicola insolens cellulases were shown to be much more sensitive to anionic surfactant than T. reesei cellulases. The use of cellulases that bind reversibly to cellulose is suggested for achieving more efficient cellulase recycling and for reducing backstaining by dye-cellulase complexes.

Adsorption↗

PubMedDate not supplied

The effect of additives and mechanical agitation in surface modification of acrylic fibres by cutinase and esterase.

The surface of an acrylic fibre containing about 7% of vinyl acetate was modified using Fusarium solani pisi cutinase and a commercial esterase, Texazym PES. The effect of acrylic solvents and stabilising polyols on cutinase operational stability was studied. The half-life time of cutinase increased by 3.5-fold with the addition of 15% N,N-dimethylacetamide (DMA) and by 3-fold with 1M glycerol. The impact of additives and mechanical agitation in the protein adsorption and in the hydrolysis of vinyl acetate from acrylic fabric was investigated. The hydroxyl groups produced on the surface of the fibre were able to react specifically with Remazol Brilliant Blue R (cotton reactive dye) and to increase the colour of the acrylic-treated fabric. The best staining level was obtained with a high level of mechanical agitation and with the addition of 1% DMA. Under these conditions, the raise in the acrylic fabric colour depth was 30% for cutinase and 25% for Texazym. The crystallinity degree, determined by X-ray diffraction, was not significantly changed between control samples and samples treated with cutinase. The results showed that the outcome of the application of these enzymes depends closely on the reaction media conditions.

Acrylic Resins↗

PubMedDate not supplied

Predicting dye biodegradation from redox potentials.

Two biological approaches for decolorization of azo sulfonated dyes have been compared: reductive decolorization with the ascomycete yeast Issatchenkia occidentalis and enzymatic oxidative decolorization with Trametes villosa laccase alone or in the presence of the mediator 1-hydroxybenzotriazole. The redox potential difference between the biological cofactor involved in the reductive activity of growing cells and the azo dye is a reliable indication for the decolorization ability of the biocatalyst. A linear relationship exists between the redox potential of the azo dyes and the decolorization efficiency of enzyme, enzyme/mediator, and yeast. The less positive the anodic peak of the dye, the more easily it is degraded oxidatively with laccase. The more positive the cathodic peak of the dye, the more rapidly the dye molecule is reduced with yeast.

Algorithms↗