Enzymatic cofactor regeneration systems: A new perspective on efficiency assessment.

Nowadays, the specificity of enzymatic processes makes them more and more important every year, and their usage on an industrial scale seems to be necessary. Enzymatic cofactors, however, play a crucial part in the prospective applications of enzymes, because they are indispensable for conducting highly effective biocatalytic activities. Due to the relatively high cost of these compounds and their consumption during the processes carried out, it has become crucial to develop systems for cofactor regeneration.

Enzymatic membrane reactor in xylose bioconversion with simultaneous cofactor regeneration.

In this study, we present the concept of co-immobilization of xylose dehydrogenase and alcohol dehydrogenase from Saccharomyces cerevisiae on an XN45 nanofiltration membrane for application in the process of xylose bioconversion to xylonic acid with simultaneous cofactor regeneration and membrane separation of reaction products. During the research, the effectiveness of the co-immobilization of enzymes was confirmed, and changes in the properties of the membrane after the processes were determined. Using the obtained biocatalytic system it was possible to obtain 99% xylonic acid production efficiency under optimal conditions, which were 5 mM xylose, 5 mM formaldehyde, ratio of NAD+:NADH 1:1, and 60 min of reaction.

Biocatalytic System Made of 3D Chitin, Silica Nanopowder and Horseradish Peroxidase for the Removal of 17α-Ethinylestradiol: Determination of Process Efficiency and Degradation Mechanism.

The occurrence of 17α-ethinylestradiol (EE2) in the environment and its removal have drawn special attention from the scientific community in recent years, due to its hazardous effects on human and wildlife around the world. Therefore, the aim of this study was to produce an efficient enzymatic system for the removal of EE2 from aqueous solutions. For the first time, commercial silica nanopowder and 3D fibrous chitinous scaffolds from marine sponge were used as supports for horseradish peroxidase (HRP) immobilization.

3D Chitin Scaffolds from the Marine Demosponge as a Support for Laccase Immobilization and Its Use in the Removal of Pharmaceuticals.

For the first time, 3D chitin scaffolds from the marine demosponge were used for adsorption and immobilization of laccase from . The resulting chitin-enzyme biocatalytic systems were applied in the removal of tetracycline. Effective enzyme immobilization was confirmed by scanning electron microscopy.

Co-Immobilization of Glucose Dehydrogenase and Xylose Dehydrogenase as a New Approach for Simultaneous Production of Gluconic and Xylonic Acid.

The conversion of biomass components catalyzed via immobilized enzymes is a promising way of obtaining valuable compounds with high efficiency under mild conditions. However, simultaneous transformation of glucose and xylose into gluconic acid and xylonic acid, respectively, is an overlooked research area. Therefore, in this work we have undertaken a study focused on the co-immobilization of glucose dehydrogenase (GDH, EC 1.

Laccase Immobilized onto Zirconia⁻Silica Hybrid Doped with Cu as an Effective Biocatalytic System for Decolorization of Dyes.

Nowadays, novel and advanced methods are being sought to efficiently remove dyes from wastewaters. These compounds, which mainly originate from the textile industry, may adversely affect the aquatic environment as well as living organisms. Thus, in presented study, the synthesized ZrO-SiO and Cu-doped ZrO-SiO oxide materials were used for the first time as supports for laccase immobilization, which was carried out for 1 h, at pH 5 and 25 °C.

Bioconversion of xylose to xylonic acid via co-immobilized dehydrogenases for conjunct cofactor regeneration.

Enzymatic cofactor-dependent conversion of monosaccharides can be used in the bioproduction of value-added compounds. In this study, we demonstrate co-immobilization of xylose dehydrogenase (XDH, EC 1.1.