A bienzymatic biocatalyst constituted by glucose oxidase and Horseradish peroxidase immobilized on ordered mesoporous silica

It is presently extremely challenging to realize an active immobilized multi-enzyme biocatalyst which allows to run in vitro multi-step cascade reactions. This work deals with the obtainment of a bienzymatic immobilized biocatalyst constituted by Glucose Oxidase (GOx) and Horseradish Peroxidase (HRP) immobilized onto SBA-15 mesoporous silica. The effect of co-immobilization (GOx/HRP@SBA-15) versus the separated immobilization (GOx@SBA-15/HRP@SBA-15), and the effect of covalent versus physical immobilization, on protein loading and enzymatic activity were investigated. Regardless the different immobilization strategy used, it was found that the catalytic activity could be retained only if the immobilized bienzymatic biocatalyst was kept wet. The obtained wet GOx/HRP@SBA-15 biocatalyst could be recycled 14 times keeping a good activity. Finally, the bienzymatic biocatalyst was tested for the oxidation of two model phenolic (caffeic acid and ferulic acid) pollutants of agricultural wastewaters, as olive mill wastewaters (OMWs). The biocatalyst was able to reach a 70% conversion within 15 min

Omics approaches to understanding the efficacy and safety of disease-modifying treatments in multiple sclerosis

From the perspective of precision medicine, the challenge for the future is to improve the accuracy of diagnosis, prognosis, and prediction of therapeutic responses through the identification of biomarkers. In this framework, the omics sciences (genomics, transcriptomics, proteomics, and metabolomics) and their combined use represent innovative approaches for the exploration of the complexity and heterogeneity of multiple sclerosis (MS). This review examines the evidence currently available on the application of omics sciences to MS, analyses the methods, their limitations, the samples used, and their characteristics, with a particular focus on biomarkers associated with the disease state, exposure to disease-modifying treatments (DMTs), and drug efficacies and safety profiles

Lactate Regulates Metabolic and Proinflammatory Circuits in Control of T Cell Migration and Effector Functions

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Glassy Carbon Electrodes Modified with Ordered Mesoporous Silica for the Electrochemical Detection of Cadmium Ions

Four different samples of ordered mesoporous silica powders (MCM-41 and SBA-15) and amino-functionalized mesoporous silica (MCM-41-NH2 and SBA-15-NH2) were used to prepare modified glassy carbon electrodes coated with ion-exchange polymer Nafion to be used for the electrochemical detection of Cd(II). The mesoporous silica samples were characterized through transmission electron microscopy, small-angle X-ray scattering, and N2-adsorption/desorption isotherms. The electrodes were characterized by using square wave anodic stripping voltammetry. The effect of pH and of the silica type on the electrodes' response was investigated. The influence of amino functional groups grafted on the silica surface toward Cd(II) ion detection was also examined. The detection limits determined with the new silica-modified electrodes [between 0.36 and 1.68 μM Cd(II)] are slightly higher than those reported in the literature, but they are lower than those stipulated in the European legislation [45 μM Cd(II)] and, consequently, the electrodes could be successfully used to detect Cd(II) in aqueous solutions

Are specific buffer effects the new frontier of Hofmeister phenomena? Insights from lysozyme adsorption on ordered mesoporous silica

Lysozyme adsorption on mesoporous silica at pH 7.15 is buffer specific. The synergistic action of buffers and salts induces relevant effects on the charged interfaces, and thus on lysozyme loading. These findings, rising doubts on the validity of the Henderson-Hasselbalch equation, suggest the occurrence of Hofmeister phenomena also for buffers

L'impasto bruno tornito

L'impasto bruno orientalizzant

Lipase and Laccase Encapsulated on Zeolite Imidazolate Framework: Enzyme Activity and Stability from Voltammetric Measurements

Lipase (Pseudomonas fluorescens) and laccase (Trametates versicolor) were encapsulated on two zeolite imidazolate framework, ZIF‐8 and ZIF‐zni, materials using a one‐pot synthesis‐immobilization method in aqueous solution at room temperature. The synthesized immobilized biocatalysts (Lip@ZIF‐8, Lip@ZIF‐zni, Lac@ZIF‐8, and Lac@ZIF‐zni) were characterized by X‐ray diffraction, scanning electron microscopy, Fourier transform infrared spectroscopy, and thermogravimetric analysis. The enzymatic activities of the four immobilized biocatalysts were characterized via the electrochemical detection of the substrates, p‐nitrophenyl butyrate and 2,2‐azinobis‐3‐ethylbenzthiazoline‐6‐sulfonic acid. For Lip@ZIF‐8 the specific activity was 91.9 U mg−1 and 123.1 U mg−1 for Lip@ZIF‐zni, while for Lac@ZIF‐8 and Lac@ZIF‐zni, the activity was 51 U mg−1 and 163 U mg−1, respectively, confirming that laccase retains a higher level of activity when immobilized onto ZIF‐zni than on ZIF‐8. Lac@ZIF‐8 was the most stable system on storage (15 days at 5 °C), retaining 94 % of initial activity, while Lip@ZIF‐zni biocatalyst had the optimal level of reusability, retaining 40 % of initial activity after five reaction cycles