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Stability and decolourization ability of trametes villosa laccase in liquid ult...

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 ...

Cotton fabric : a natural matrix suitable for controlled release systems

The possibility to use cotton as a matrix for controlled release systems was studied by covalently attaching a model compound, specifically the reactive dye Remazol Brilliant Blue R to its surface. Afterwards the fabric was coated with a commercial cellulase. The release of the dye, obtained by the hydrolysis of cotton fibres in sweat buffer, was monitored. The reducing sugars concentration increased for both f...

Optimisation of a serine protease coupling to Eudragit S-100 by experimental de...

A full factorial design was used to study the influence of four different variables, namely polymer concentration, carbodiimide concentration, time of reaction and blocking agent concentration, on the coupling of a serine protease into a soluble–insoluble polymer (Eudragit S-100). All of the four factors studied have played a critical role in the protease coupling. Response surface methodology was used as an op...

Immobilization of proteases with a water soluble–insoluble reversible polymer f...

A commercial protease, Esperase, was covalently linked to Eudragit S-100, a reversible soluble–insoluble polymer by carbodiimide coupling. When compared to the native enzyme, the immobilized form presented a lower specific activity towards high molecular weight substrates but a higher thermal stability at all temperatures tested. The optimum pH of the immobilized protease was shifted towards the alkaline side b...

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...

Specificities of a chemically modified laccase from trametes

Laccases could prevent fabrics and garments from re-deposition of dyes during washing and finishing processes by degrading the solubilized dye. However, laccase action must be restricted to solubilized dye molecules thereby avoiding decolorization of fabrics. Chemical modification of enzymes can provide a powerful tool to change the adsorption behaviour of enzymes on water insoluble polymers. Polyethylene glyco...

Restricting detergent protease action to surface of protein fibres by chemical ...

Due to their excellent properties, such as thermostability, activity over a broad range of pH and efficient stain removal, proteases from Bacillus sp. are commonly used in the textile industry including industrial processes and laundry and represent one of the most important groups of enzymes. However, due to the action of proteases, severe damage on natural protein fibres such as silk and wool result after was...

Treatment of wool fibres with subtilisin and subtilisin-PEG

In this work the diffusion of serine proteases into wool fabrics and yarns was studied. The proteases used were free subtilisin and subtilisin-PEG (the same enzyme that was covalently cross linked to polyethylene glycol). It is shown that the adsorption and diffusion is facilitated by the pre-treatment performed, being the alkaline surfactant washing and bleaching the most effective in what concerns enzyme adso...

Enzymatic treatment of wool with modified proteases

Tese de doutoramento em Engenharia Têxtil. ; The tendency of wool to felt and shrink is mainly due to its scaly structure. The chlorine-Hercosett is the most widespread process used to modify the scales of wool fibres with the purpose of providing resistance to felting and shrinkage. There have been many attempts to replace this chlorine process by an environmental friendly enzymatic process that wouid similar...

Chemical modifications on proteins using glutaraldehyde