Sara C. Silvério

Bio: Sara C. Silvério is an academic researcher from University of Minho. The author has contributed to research in topics: Prebiotic & Aqueous two-phase system. The author has an hindex of 18, co-authored 45 publications receiving 784 citations. Previous affiliations of Sara C. Silvério include University of Porto & Faculdade de Engenharia da Universidade do Porto.

Green coconut fiber: a novel carrier for the immobilization of commercial laccase by covalent attachment for textile dyes decolourization

Abstract: Commercial laccase formulation was immobilized on modified green coconut fiber silanized with 3-glycidoxypropyltrimethoxysilane, aiming to achieve a cheap and effective biocatalyst. Two different strategies were followed: one point (pH 7.0) and multipoint (pH 10.0) covalent attachment. The influence of immobilization time on enzymatic activity and the final reduction with sodium borohydride were evaluated. The highest activities were achieved after 2 h of contact time in all situations. Commercial laccase immobilized at pH 7.0 was found to have higher activity and higher affinity to the substrate. However, the immobilization by multipoint covalent attachment improved the biocatalyst thermal stability at 50 °C, when compared to soluble enzyme and to the immobilized enzyme at pH 7.0. The Schiff’s bases reduction by sodium borohydride, in spite of causing a decrease in enzyme activity, showed to contribute to the increase of operational stability through bonds stabilization. Finally, these immobilized enzymes showed high efficiency in the continuous decolourization of reactive textile dyes. In the first cycle, the decolourization is mainly due to dyes adsorption on the support. However, when working in successive cycles, the adsorption capacity of the support decreases (saturation) and the enzymatic action increases, indicating the applicability of this biocatalyst for textile wastewater treatment.

Effect of Aqueous Two-Phase System Constituents in Different Poly(ethylene glycol)–Salt Phase Diagrams

Abstract: Eight different poly(ethylene glycol) (PEG)/salt aqueous two-phase systems (ATPS's) were characterized at 23 °C. PEGs with different molecular weights (1500 and 8000) were combined with different salts (sodium or potassium citrates and formates) to study the effect of each ATPS constituent in the phase diagram. The binodal curve and several tie-lines were determined for each system using common analytical techniques described in the literature for ATPS's (cloud point method, conductivity, and gravimetric analysis after lyophilization). According to the results, it was found that each ATPS constituent produced a particular effect in the phase diagram. For the salts, changes in the anion produced larger variations in the heterogeneous region size than changes of the cation. Thus, the effect of salt type seems to be largely dependent on the anion, which makes the dominant contribution. The ability to form ATPS's is connected with the Gibbs energy of hydration, ΔGhyd, of the anions: more negative ΔGhyd values...

The Effect of Salts on the Liquid−Liquid Phase Equilibria of PEG600 + Salt Aqueous Two-Phase Systems

Abstract: Six new ATPSs were prepared by combining polyethylene glycol PEG600 with potassium citrate, dipotassium hydrogen phosphate, sodium formate, potassium formate, sodium sulfate, and lithium sulfate. Complete phase diagrams, including the binodal curve and three tie-lines, were determined at 23 °C. The experimental data obtained for the binodal curve were successfully adjusted to the Merchuk equation, and the reliability of tie-line data was confirmed using the equations suggested by Othmer–Tobias and Bancroft. The ability of each ion to induce ATPS formation was investigated. Na+ proved to be more effective in ATPS formation than K+ and Li+. For potassium salts, the order observed for the effectiveness of the anions was: HPO42– > C6H5O73– > HCO2–. Regarding the sodium salts, it was found that SO42– is clearly more effective than HCO2–. The position of the ions in the Hofmeister series and their free energy of hydration (ΔGhyd) were used to explain the ability of the ions to induce PEG salting-out. Furthermor...

Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases

Abstract: The main objective of the immobilization of enzymes is to enhance the economics of biocatalytic processes Immobilization allows one to re-use the enzyme for an extended period of time and enables easier separation of the catalyst from the product Additionally, immobilization improves many properties of enzymes such as performance in organic solvents, pH tolerance, heat stability or the functional stability Increasing the structural rigidity of the protein and stabilization of multimeric enzymes which prevents dissociation-related inactivation In the last decade, several papers about immobilization methods have been published In our work, we present a relation between the influence of immobilization on the improvement of the properties of selected oxidoreductases and their commercial value We also present our view on the role that different immobilization methods play in the reduction of enzyme inhibition during biotechnological processes

From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes.

Abstract: Enzymes found in nature have been exploited in industry due to their inherent catalytic properties in complex chemical processes under mild experimental and environmental conditions. The desired industrial goal is often difficult to achieve using the native form of the enzyme. Recent developments in protein engineering have revolutionized the development of commercially available enzymes into better industrial catalysts. Protein engineering aims at modifying the sequence of a protein, and hence its structure, to create enzymes with improved functional properties such as stability, specific activity, inhibition by reaction products, and selectivity towards non-natural substrates. Soluble enzymes are often immobilized onto solid insoluble supports to be reused in continuous processes and to facilitate the economical recovery of the enzyme after the reaction without any significant loss to its biochemical properties. Immobilization confers considerable stability towards temperature variations and organic solvents. Multipoint and multisubunit covalent attachments of enzymes on appropriately functionalized supports via linkers provide rigidity to the immobilized enzyme structure, ultimately resulting in improved enzyme stability. Protein engineering and immobilization techniques are sequential and compatible approaches for the improvement of enzyme properties. The present review highlights and summarizes various studies that have aimed to improve the biochemical properties of industrially significant enzymes.

Handbook Of Proteolytic Enzymes

Abstract: Thank you very much for downloading handbook of proteolytic enzymes. Maybe you have knowledge that, people have search hundreds times for their favorite books like this handbook of proteolytic enzymes, but end up in infectious downloads. Rather than reading a good book with a cup of tea in the afternoon, instead they cope with some harmful bugs inside their computer. handbook of proteolytic enzymes is available in our book collection an online access to it is set as public so you can get it instantly. Our book servers spans in multiple locations, allowing you to get the most less latency time to download any of our books like this one. Kindly say, the handbook of proteolytic enzymes is universally compatible with any devices to read.

Bacterial versus fungal laccase: potential for micropollutant degradation

Abstract: Relatively high concentrations of micropollutants in municipal wastewater treatment plant (WWTP) effluents underscore the necessity to develop additional treatment steps prior to discharge of treated wastewater. Microorganisms that produce unspecific oxidative enzymes such as laccases are a potential means to improve biodegradation of these compounds. Four strains of the bacterial genus Streptomyces (S. cyaneus, S. ipomoea, S. griseus and S. psammoticus) and the white-rot fungus Trametes versicolor were studied for their ability to produce active extracellular laccase in biologically treated wastewater with different carbon sources. Among the Streptomyces strains evaluated, only S. cyaneus produced extracellular laccase with sufficient activity to envisage its potential use in WWTPs. Laccase activity produced by T. versicolor was more than 20 times greater, the highest activity being observed with ash branches as the sole carbon source. The laccase preparation of S. cyaneus (abbreviated LSc) and commercial laccase from T. versicolor (LTv) were further compared in terms of their activity at different pH and temperatures, their stability, their substrate range, and their micropollutant oxidation efficiency. LSc and LTv showed highest activities under acidic conditions (around pH 3 to 5), but LTv was active over wider pH and temperature ranges than LSc, especially at near-neutral pH and between 10 and 25°C (typical conditions found in WWTPs). LTv was also less affected by pH inactivation. Both laccase preparations oxidized the three micropollutants tested, bisphenol A, diclofenac and mefenamic acid, with faster degradation kinetics observed for LTv. Overall, T. versicolor appeared to be the better candidate to remove micropollutants from wastewater in a dedicated post-treatment step.