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10 results for “enzyme immobilization”
Three-Enzyme Phosphorylase Cascade Immobilized on Solid Support for Biocatalytic Synthesis of Cello-oligosaccharides
<p>We provide here the underlying data of the scientific publication "Three-Enzyme Phosphorylase Cascade Immobilized on Solid Support for Biocatalytic Synthesis of Cello-oligosaccharides". Please find the abstract below:</p> <p>Enzyme cascades are promising for multistep biocatalytic synthesis, but their effective use beyond the proof-of-concept stage is challenging. Strategies to recycle the individual enzymes are critical for the applicability of such cascades. Immobilization on solid support is well developed for single enzymes but remains difficult for enzyme ensembles. Here, we show a controlled co-immobilization of three glycoside phosphorylases to establish a highly active and recyclable biocatalyst for the conversion of sucrose and glucose into soluble (short-chain) cello-oligosaccharides. We use protein fusion with the binding module Z<sub>basic2 </sub>to enable non-covalent surface tethering of all enzymes according to a uniform principle and in a programmable fashion. We thus achieve loading of the phosphorylases in an activity ratio optimal for the overall conversion rate and for controlling the cello-oligosaccharide chain length (≤ 6), hence the solubility, in the reaction. We demonstrate efficient production of ~12 g/L cello-oligosaccharides in 5 reaction cycles with integrated enzyme re-use. This study presents a major advance toward the practical use of systems bio-catalysis on solid support.</p>
TERMINUS WP4: Enzyme immobilization, protection, and triggering. TASK 4.2: Experimental data
<p>A. E. Delorme, J.-M. Andanson and V. Verney: Improving Laccase Thermostability with aqueous Natural Deep Eutectic Solvents, <em>Int. J. Biol. Macromol.</em>, (2020), <a href="https://doi.org/10.1016/j.ijbiomac.2020.07.022">doi.org/10.1016/j.ijbiomac.2020.07.022</a></p> <p><strong>Abstract</strong></p> <p>The wide-spread use of laccases in industry is often limited due to the enzyme inactivation over time at conditions which exceeds the operating conditions of the enzymes, which are neutral pH and ambient temperatures (30-40 °C). Today, the most common strategies used to improve enzyme stability are chemical modifications and immobilization of enzymes on solid supports. Although, these techniques have shown promise in improving enzyme stability, they are often synthetically demanding and unsustainable in terms of costs and synthesis route. Deep Eutectic Solvents (DESs) have attracted considerable attention as reaction media in biocatalysis due to their promising compatibility with enzymes and sustainable derivation. In this contribution we demonstrate the possibility of applying DESs as incubation media to inhibit thermal inactivation of laccase T. Versicolor. For example we show that by incubating laccase in 25 wt% of a betaine-xylitol based DES at 70 °C for 15 minutes, the measured residual activity of laccase is a near 10 fold greater than the measured residual activity of laccase when incubated without the DES. The drastic enhancement of the enzyme thermostability by pre-incubation of laccase in DES media showcases a facile, cheap and green method of boosting the stability laccase.</p> <p> </p> <p><strong>Dataset</strong></p> <p>This dataset contains all the UV-kinetic raw data used to calculate the laccase activity in the article “Improving Laccase Thermostability with aqueous Natural Deep Eutectic Solvents”. Data are available in a compressed .zip file with 1 folder (Laccase-thermostability-DES_v1.0_TER_WP4_D4-2) containing 3 files:</p> <p> </p> <ul> <li>one tabular file saved in .xlsx format containing all UV-kinetic raw data used to calculate the relative and residual laccase activities for figure 1-6 in the article (<a href="https://doi.org/10.1016/j.ijbiomac.2020.07.022">doi.org/10.1016/j.ijbiomac.2020.07.022</a>). The Laccase-thermostability-DES_v1.0_TER_WP4_D4-2.xlsx file contains the UV kinetic absorption spectra (at wavelength 417 nm) and each row in represent one spectrum. The spectra are grouped under laccase incubation temperature and length of time of incubation. For each incubation time, three solutions were prepared which signifies the three trials under each incubation times. Each sheet in the .xlsx file represent the data set collected for each laccase incubation medium</li> <li>The Materials_and_experimental_method-D4-2-Laccase-Thermostability-DES.pdf file details the experimental method and conditions for the data acquisition presented in the Laccase-thermostability-DES_v1.0_TER_WP4_D4-2.xlsx. Guidance is also provided on how to use the data to calculate the laccase activity and thermostability.</li> <li>The_metadata_information-D4-2-Laccase-Thermostability-DES.pdf includes more detailed metadata information for the dataset represented in the excel file Laccase-thermostability-DES_v1.0_TER_WP4_D4-2.xlsx.</li> </ul>
TERMINUS WP4 Enzyme immobilization, protection, and triggering. TASK 4.1 TASK 4.2 Experimental data – Hydrolytic enzyme immobilization and triggering
<p>The use of polymer-degrading enzymes is an attractive and effective method for the management of plastic waste. Synthetic polyesters such as poly(ethylene terephthalate) (PET) or polyurethane (PUR) have been shown to be susceptible to enzymatic degradation by microbial polyester hydrolases, as well as biopolyesters such as poly(lactic acid) (PLA), poly(butylene succinate) (PBS), and polycaprolactone (PCL). However, raw enzymes are not used in polymer formulations because the high processing temperatures would deteriorate the proteins (whose enzymes are made of), by destroying their macromolecular structure and catalytic center. The possibility of a direct use of enzyme in a polymer formulation thorough an opportune protective system, able to preserve the activity of the enzyme and increase its thermal stability, could open to new materials degradable “on-demand” at the end-of life. Therefore, significant progresses could be possible for example in the field of plastic packaging, which currently represents 40% of the total production of plastic in EU and requires the consumption of more than 19 million tons of oil and gas.</p> <p>This dataset includes some of the experimental raw data presented by UNIBO in deliverable D4.1 and D4.3, namely FT-IR analysis, X-ray diffraction analysis, TGA analysis, UV-Vis spectrophotometer. Data are available in a compressed .zip file with 1 folder (Hydrolytic enzyme immobilization and triggering_v1.0_TER_WP4_D4.1_D4.3) containing 6 files, 4 .xlsx files containing the FT-IR, XRD, TGA, Enzyme release kinetics and Thermostability raw data, 1 .pdf file describing the experimental methods and materials and a second .pdf file outlining the metadata and information.</p> <p>1_Hydrolytic enzyme immobilization and triggering _FTIR.xlsx contains all the FTIR raw data and curves of the Immobilized enzyme systems prepared.</p> <p>2_Hydrolytic enzyme immobilization and triggering _XRD.xlsx contains all the XRD raw data and profiles of the Immobilized enzyme systems prepared.</p> <p>3_Hydrolytic enzyme immobilization and triggering _TGA.xlsx contains all the TGA raw data and curves of the Immobilized enzyme systems prepared.</p> <p>4_Hydrolytic enzyme immobilization and triggering release activity and thermal resistance.xlsx contains all the raw data and graphs related to the protein content, activity of the Immobilized enzyme systems prepared after release and the thermal stress experiment data.</p> <p>Materials and experimental method_D4.1_D4.3_Hydrolytic enzyme immobilization and triggering.pdf contains the details of the experimental method and conditions for the data acquisition presented in the data set.</p> <p>Metadata information for WP4 dataset_D4.1_D4.3_Hydrolytic enzyme immobilization and triggering.pdf includes more detailed metadata information for the dataset presented.</p>
2,5-Furandicarboxaldehyde as a Bio-based Crosslinking Agent Replacing Glutaraldehyde for Covalent Enzyme Immobilization
<p>In the quest for a bio-based and safer substitute for glutaraldehyde, we have investigated 2,5 diformylfuran (DFF) as bifunctional crosslinking agent for the covalent immobilization of glucoamylase on amino-functionalized methacrylic resins. Immobilization experiments and systematic comparison with glutaraldehyde at four different concentrations for the activation step showed that DFF leads to comparable enzymatic activities at all tested concentrations. Continuous flow experiment confirms a similar long term stability of the immobilized formulations obtained with the two crosslinkers. The NMR study of DFF in aqueous solution evidenced a much simpler behaviour as compared to glutaraldehyde, since no enolic forms can form and only a mono-hydrated form was observed. Unlike in the case of glutaraldehyde, DFF reacts covalently with the primary amino groups <em>via</em> imine bond formation only. Nevertheless, the stability of the covalent immobilization was confirmed also at acidic pH (4.5), most probably because of the higher stability of the imine bonds formed with the aromatic aldehydes. In terms of toxicity DFF has the advantage of being poorly soluble in water and, more importantly, poorly volatile as compared to glutaraldehyde, which displays severe respiratory toxicity. We have performed preliminary ecotoxicity assays using <em>Aliivibrio fischeri</em>, a marine bacterium, evidencing comparable behaviour (below the toxicity threshold) for both dialdehydes at the tested concentrations.</p>
Figure 1 in Recent progress in magnetic nanoparticles and mesoporous materials for enzyme immobilization: an update
Figure 1. Mesoporous material-functioned MNPs.
Research data supporting "Rolling Circle Transcription-Amplified Hierarchically Structured Organic-Inorganic Hybrid RNA Flowers for Enzyme Immobilization""
<p>Raw research data supporting the publication:</p> <p>Wang Y. et al., 2019, ACS Applied Materials and Interfaces, DOI: 10.1021/acsami.9b04663</p>
The Alginate Immobilization of Metabolic Enzymes (AIME) platform retrofits an estrogen receptor transactivation assay with metabolic competence
The U.S. EPA Endocrine Disruptor Screening Program utilizes data across the ToxCast/Tox21 high-throughput screening (HTS) programs to evaluate the biological effects of potential endocrine active substances (EAS). A potential limitation to the use of in vitro assay data in regulatory decision-making is the lack of coverage for xenobiotic metabolic processes. Both hepatic- and peripheral-tissue metabolism can yield metabolites that exhibit greater activity than the parent compound (bioactivation) or are inactive (bioinactivation) for a given biological target. Interpretation of biological effect data for both putative EAS, as well as other chemicals, screened in HTS assays may benefit from the addition of xenobiotic metabolic capabilities to decrease the uncertainty in predicting potential hazards to human health. The objective of this study was to develop an approach to retrofit existing HTS assays with hepatic metabolism. The Alginate Immobilization of Metabolic Enzymes (AIME) platform encapsulates hepatic S9 fractions in alginate microspheres attached to 96-well peg lids. Functional characterization across a panel of reference substrates for phase I cytochrome P450 enzymes revealed substrate depletion with expected metabolite accumulation. Performance of the AIME method in the VM7Luc estrogen receptor (ER) transactivation assay was evaluated across 15 reference chemicals and 48 test chemicals that yield metabolites previously identified as ER active or inactive. The results demonstrate the utility of applying the AIME method for identification of false positive and false negative target assay effects, reprioritization of hazard based on metabolism-dependent bioactivity, and enhanced in vivo concordance with the rodent uterotrophic bioassay. Integration of the AIME metabolism method may prove useful for future biochemical and cell-based HTS applications.
The Alginate Immobilization of Metabolic Enzymes (AIME) platform retrofits an estrogen receptor transactivation assay with metabolic competence
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Enzyme Immobilization with Plant-based Polysaccharides through Complex Coacervation
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Figure 3 in Recent progress in magnetic nanoparticles and mesoporous materials for enzyme immobilization: an update
Figure 3. Enzyme immobilization on mesoporous materials.
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