An assessment of CFD applied to steady flow in a planar diffuser upstream of an automotive catalyst

Flow maldistribution across automotive exhaust catalysts significantly affects their conversion efficiency. Flow behaviour can be predicted using computational fluid dynamics (CFD). This study investigates the application of CFD to modelling flow in a 2D system consisting of a catalyst monolith downstream of a wide-angled planar diffuser presented with steady flow. Two distinct approaches, porous medium and individual channels, are used to model monoliths of length 27 mm and 100 mm. Flow predictions are compared to particle image velocimetry (PIV) measurements made in the diffuser and hot wire anemometry (HWA) data taken downstream of the monolith. Both simulations compare favourably with PIV measurements, although the models underestimate the degree of mixing in the shear layer at the periphery of the emerging jet. Tangential velocities are predicted well in the central jet region but are overestimated elsewhere, especially at the closest measured distance, 2.5 mm from the monolith. The individual channels model is found to provide a more consistently accurate velocity profile downstream of the monolith. Maximum velocities, on the centre line and at the secondary peak near to the wall, are reasonably well matched for the cases where the flow is more maldistributed. Under these conditions, a porous medium model remains attractive because of low computational demand

Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions

L-asparaginases (EC 3.5.1.1) are a family of enzymes that catalyze the hydrolysis of L-asparagine to L-aspartic acid and ammonia. These proteins with different biochemical, physicochemical and pharmacological properties are found in many organisms, including bacteria, fungi, algae, plants and mammals. To date, asparaginases from E. coli and Dickeya dadantii (formerly known as Erwinia chrysanthemi) are widely used in hematology for the treatment of lymphoblastic leukemias. However, their medical use is limited by side effects associated with the ability of these enzymes to hydrolyze L-glutamine, as well as the development of immune reactions. To solve these issues, gene-editing methods to introduce amino-acid substitutions of the enzyme are implemented. In this review, we focused on molecular analysis of the mechanism of enzyme action and to optimize the antitumor activity

Influence of cyclic variance on the performance of URANS for pulsating flow upstream of an automotive catalyst monolith

CFD predictions using the URANS equations have been compared to phase-averaged and instantaneous PIV pulsating flow fields in a planar diffuser upstream of a catalyst monolith. URANS qualitatively capture the velocity and vorticity fields, in particular the spatial and temporal evolution of the main vortices in the diffuser during the acceleration phase of the cycle. However, they over-predict vortex intensity and hence its residual strength at the beginning of successive pulses. Instantaneous PIV measurements show there is a significant cycle-to-cycle variation in the position and structure of the vortices within the diffuser. This serves to "diffuse" the phase-averaged vortex strength. Alternative simulation techniques such as LES or DNS will be needed if the cyclic variation is to be correctly predicted as this will affect conversion efficiency

Improvement of Biocatalytic Properties and Cytotoxic Activity of L-Asparaginase from Rhodospirillum rubrum by Conjugation with Chitosan-Based Cationic Polyelectrolytes

L-asparaginases (L-ASNases, EC 3.5.1.1) are a family of enzymes that are widely used for the treatment of lymphoblastic leukemias. L-ASNase from Rhodospirillum rubrum (RrA) has a low molecular weight, low glutaminase activity, and low immunogenicity, making it a promising enzyme for antitumor drug development. In our work, the complex formation and covalent conjugation of the enzyme with synthetic or natural polycationic polymers was studied. Among non-covalent polyelectrolyte complexes (PEC), polyethyleneimine (PEI) yielded the highest effect on RrA, increasing its activity by 30%. The RrA-PEI complex had increased stability to trypsinolysis, with an inactivation constant decrease up to 10-fold compared to that of the native enzyme. The covalent conjugation of RrA with chitosan-PEI, chitosan-polyethylene glycol (chitosan-PEG), and chitosan-glycol resulted in an increase in the specific activity of L-asparagine (up to 30%). RrA-chitosan-PEG demonstrated dramatically (by 60%) increased cytotoxic activity for human chronic myeloma leukemia K562 cells in comparison to the native enzyme. The antiproliferative activity of RrA and its conjugates was significantly higher (up to 50%) than for that of the commercially available EcA at the same concentration. The results of this study demonstrated that RrA conjugates with polycations can become a promising strategy for antitumor drug development

L-Asparaginase Conjugates from the Hyperthermophilic Archaea <i>Thermococcus sibiricus</i> with Improved Biocatalytic Properties

This study investigated the effect of polycationic and uncharged polymers (and oligomers) on the catalytic parameters and thermostability of L-asparaginase from Thermococcus sibiricus (TsA). This enzyme has potential applications in the food industry to decrease the formation of carcinogenic acrylamide during the processing of carbohydrate-containing products. Conjugation with the polyamines polyethylenimine and spermine (PEI and Spm) or polyethylene glycol (PEG) did not significantly affect the secondary structure of the enzyme. PEG contributes to the stabilization of the dimeric form of TsA, as shown by HPLC. Furthermore, neither polyamines nor PEG significantly affected the binding of the L-Asn substrate to TsA. The conjugates showed greater maximum activity at pH 7.5 and 85 °C, 10–50% more than for native TsA. The pH optima for both TsA-PEI and TsA-Spm conjugates were shifted to lower pH ranges from pH 10 (for the native enzyme) to pH 8.0. Additionally, the TsA-Spm conjugate exhibited the highest activity at pH 6.5–9.0 among all the samples. Furthermore, the temperature optimum for activity at pH 7.5 shifted from 90–95 °C to 80–85 °C for the conjugates. The thermal inactivation mechanism of TsA-PEG appeared to change, and no aggregation was observed in contrast to that of the native enzyme. This was visually confirmed and supported by the analysis of the CD spectra, which remained almost unchanged after heating the conjugate solution. These results suggest that TsA-PEG may be a more stable form of TsA, making it a potentially more suitable option for industrial use