The insolubilization of a recombinant l-arabinose isomerase (l-AI) from Enterococcus faecium by cross-linked enzyme aggregates (CLEA) was investigated, aiming the biochemical production of d-tagatose from d-galactose.  https://www.selleckchem.com/products/ABT-263.html  d-tagatose is a functional sweetener that has many health benefits, sweetening properties and lower calorific value. Different precipitants (ammonium sulfate, ethanol, acetone, polyethylene glycol 4000) were used in the first step of the protocol, in order to establish the precipitation conditions, and the best results of yield and activity were achieved with ammonium sulfate. In order to facilitate the recovery of the biocatalyst, a new strategy for immobilization of the multimeric enzyme l-arabinose isomerase was proposed. Magnetic cross-linked enzyme aggregates (m-CLEA) were obtained using ammonium sulfate as precipitant and magnetic nanoparticles (MNP) functionalized with APTES (3- Aminopropyltriethoxysilane). Another immobilization strategy was to immobilize the enzyme onto MNP-APTES, as a control. The best results were achieved when the m-CLEA was produced with 20 mg of MNP, 7.69 U. g-1 of enzymatic activity, 7.61 % of recovered activity, 99 % of yield of immobilization. On the other hand, the enzyme immobilized onto MNP-APTES, presented only 2.12 U. g-1 of enzymatic activity, 32.3 % of recovered activity, and 15 % of yield of immobilization.Cheese lacks essential fatty acids (EFAs). Delta 12 fatty acid desaturase (FADS12) is a critical enzyme required for EFA biosynthesis in fermentation of the predominant strains of cheese. Previously, we identified the FADS12 gene and characterized its function for the first time in Geotrichum candidum, a dominant strain used to manufacture soft cheese with white rind. In this study, we analyzed the molecular mechanism of FADS12 function by swapping domains from Mortierella alpina and G. candidum that had, respectively, high and low oleic acid conversion rates. The results revealed three regions that are essential to this process, including regions from the end of the second transmembrane domain to the beginning of the third transmembrane domain, from the end of the third transmembrane domain to the beginning of the fourth transmembrane domain, and from the 30-amino acid from the end of the sixth transmembrane domain to the C-terminal end region. Based on our domain swapping analyses, nine pairs of amino acidsponsible for the catalytic activity of FADS12 at various temperatures, pH, and times. This study offers a solid theoretical basis to develop preconditioning methods to increase the rate at which GcFADS12 converts oleic and linoleic acids to produce higher levels of EFAs in cheese.The benzazoles are very important entities having immense biological activities, hence; the synthesis of benzazoles is one of the prime areas for synthetic chemists. In pursuit of sustainable protocol, herein an oxidative enzyme i.e. catalase mediated sustainable synthesis is presented. Catalase is a metalloenzyme which is essential for the breakdown of toxic hydrogen peroxide into water and oxygen inside the cell. Despite the higher activity and turnover number of catalase inside the cell, its activity outside the cell is unexplored. Therefore, to explore the hidden potential of catalase for catalyzing the organic transformations, here we reported a green and efficient method for synthesis of benzazoles by the cyclocondensation of o-aminothiophenol or o-phenylenediammine and various aryl aldehydes with ensuing dehydrogenation. This protocol is greener, sustainable and rapid with excellent yields of the products and in addition to this, the catalase demonstrates good functional group tolerance.In this work, porous biochar derived from sugarcane bagasse was prepared and then coated with different amounts of chitosan (C@CS) for cellulase immobilization. Cellulase was covalently immobilized on the support by using glutaraldehyde as a linker. The chemical characteristics and morphology of the samples were determined by SEM, BET, FT-IR and XPS. The properties of immobilized enzyme were evaluated by activity recovery, optimum pH value and temperature, and recyclability. The results showed that all the three kinds of immobilized cellulase did not change the optimum pH value of 4 and temperature of 60 °C, and they also exhibited good activity and reusability. Especially for C@CS25 (the feeding ratio of porous biochar to chitosan was 0.5 g 25 mg), the support retained the morphology of porous biochar well. The corresponding immobilized cellulase kept 67 % activity of free cellulase at pH = 4 and 60 °C, and showed a glucose productivity of 90.8 % even after 10 cycles.Lipase from Thermomyces lanuginosus (TLL) was immobilized onto a novel heterofunctional support, divinyl sulfone (DVS) superparamagnetic nanoparticles (SPMNs) functionalized with polyethyleneimine (PEI). Particle size and zeta potential measurements, elemental analysis, X-ray powder diffraction, magnetic measurements, and infrared spectroscopy analysis were used to characterize the TLL preparations. At pH 10, it was possible to achieve 100 % of immobilization yield in 1 h. The immobilization pH gives TLL preparations with different stabilities; indeed the TLL preparation immobilized at pH 5.0 was the most stable during the thermal inactivation at all pH values. For the hydrolysis of racemic methyl mandelate, the nanobiocatalysts immobilized at pH 5.0 and blocked with ethylenediamine (EDA) and ethanolamine (ETA) obtained good enantioselectivities (68 % and 72 %, respectively) with high catalytic activities in the reaction medium at pH 7.0. The operational stability of the systems was evaluated in the esterification reaction of benzyl alcohol, obtaining up to 61 % conversion after the seventh reaction cycle. These results show that SPMN@PEI-DVS support is a robust strategy for the easy and rapid recovery of the nanobiocatalyst by applying a magnetic field, showing great potential for industrial applications.Living cells are constantly exposed to reactive oxygen species (ROS) causing them to rely on a constant supply of exogenous antioxidants. Quercetin (Q) is one of the potent exogenous antioxidants utilized in various antioxidant formulations. However, the potential application of Q is largely limited because of its poor water solubility. In this study, we employed titanium dioxide (TiO2) nanoparticles to maximize cellular penetration and antioxidant effect of Q on mouse fibroblast cells. To accomplish this, polyethylene glycol (PEG) modified TiO2-nanoparticle surfaces were utilized that exhibited better dispersion, with enhanced biocompatibility. Cell viability assays using Q and Q-conjugated TiO2-nanoparticles (QTiO2) were evaluated in terms of cell morphology as well as with an immunoblotting analysis to look for key biomarkers of apoptosis. In addition, cleavages of Cas 3 and PARP were obtained in cells treated with Q. Furthermore, antioxidant defence with QTiO2 was validated by means of the Nrf2 upregulation pathway.