Ana Maria Baruzzi

TL;DR: An amperometric sensor for lactate quantification requires only 0.2 U of lactate oxidase, which is immobilized in a mucin/albumin hydrogel matrix and presents remarkable operational stability and sensitivity.

TL;DR: In this article, a lactate biosensor was developed through the immobilization of lactate oxidase (LOD) in an albumin and mucin composed hydrogel, and the enzyme was then cross-linked with glutaraldehyde to the polymeric matrix and entrapped between two polycarbonate membranes.

TL;DR: In this paper, the physicochemical properties of the support may contribute to determine the analytical response of this type of sensor, and the results demonstrate that mucin induces high control for oxalate diffusion and that the interactions between mucin and carbopol molecules produce a notable gel strengthening that is reflected on the viscoelastic behavior and on the relatively smaller swelling index of the mucin/carbopol gels.

TL;DR: In this paper, the Gibbs energy of interfacial transfer of Ni(II) complexed with some selected substituted ethylenediamines which differ in hydrophobicity, is measured voltammetrically and compared with the corresponding Gibbs energy for transfer of NII with aromatic diazines, and the collected thermodynamic data allow the calculation of the stability constants of the complexes in the organic phase which are higher by five orders of magnitude than in the aqueous phase.

TL;DR: An amperometric enzyme-electrode prepared with glucose oxidase, which have been immobilized by a cross-linking step with glutaraldehyde in a mixture containing albumin and a novel carbon nanotubes- mucin composite (CNT-muc), and the storage stability was remarkable during the first 300 days.