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5 results for “Biocatalysts”
FTIR Microscopy for Direct Observation of Conformational Changes on Immobilized ω-Transaminase: Effect of Water Activity and Organic Solvent on Biocatalyst Performance
<p>Enzyme immobilization is a key strategy to expand the scope of enzyme applications and to enable the recycling of biocatalysts, resulting in greener and more cost-efficient processes. The full exploitation of the technology advantages is strictly connected to the optimal selection of the carriers and the rational development of the immobilization protocol. The present study achieved such objectives by investigating the activity of a ω-transaminase in organic solvent (toluene) upon immobilization on commercially controlled porosity glass carriers (EziG™) with diverse porosity and surface functionalization. In addition to more conventional wet-chemistry approaches and confocal microscopy, infrared microspectroscopy and imaging were exploited to highlight the enzyme distribution in a label-free manner and provide details on the immobilized enzyme's conformation with respect to the native form. Contrary to what could be expected, the highest activity of the enzyme in organic solvent was achieved for the immobilization protocol on the most hydrophilic support that more severely affects the enzyme secondary structure, promoting a beta-sheet rich folding. Experimental data show that values of water activity above 0.90 in the reaction system had a positive effect on the efficiency of the transaminase reaction. The present study represents the first example of rational development of immobilization protocols relying on direct observation of the enzyme conformation upon immobilization, shedding light on the mutual interaction between the diverse process parameters and the carrier properties.</p>
Enzymatic Cascade for the Synthesis of 2,5-Furandicarboxylic Acid in Biphasic and Microaqueous Conditions: 'Media-Agnostic' Biocatalysts for Biorefineries
<p>5-hydroxymethylfurfural (HMF) is produced upon dehydration of C6 sugars in biorefineries. As the product, it remains either in aqueous solutions, or is in situ extracted to an organic medium (biphasic system). For the subsequent oxidation of HMF to 2,5-furandicarboxylic acid (FDCA), ‘media-agnostic’ catalysts that can be efficiently used in different conditions, from aqueous to biphasic, and to organic (microaqueous) media, are of interest. Here, the concept of a one-pot biocatalytic cascade for production of FDCA from HMF was reported, using galactose oxidase (GalOx) for the formation of 2,5-diformylfuran (DFF), followed by the lipase-mediated peracid oxidation of DFF to FDCA. GalOx maintained its catalytic activity upon exposure to a range of organic solvents with only 1 % (v/v) of water. The oxidation of HMF to 2,5-diformylfuran (DFF) was successfully established in ethyl acetate-based biphasic or microaqueous systems. To validate the concept, the reaction was conducted at 5 % (v/v) water, and integrated in a cascade where DFF was subsequently oxidized to FDCA in a reaction catalyzed by <em>Candida antarctica</em> lipase B.</p>
Understanding Activity-Stability Tradeoffs in Biocatalysts by Enzyme Proximity Sequencing
<p>Data and scripts of the manuscript "<strong>Understanding Activity-Stability Tradeoffs in Biocatalysts by Enzyme Proximity Sequencing</strong>" by Rosario Vanella, Christoph Küng, Alexandre A. Schoepfer, Vanni Doffini, Jin Ren and Michael A. Nash.</p>
Production of 14α-hydroxysteroids by a recombinant Saccharomyces cerevisiae biocatalyst expressing fungal steroid 14α-hydroxylation system
GEO Series GSE128819. Curvularia lunata. 2 samples. Type: Expression profiling by high throughput sequencing.
Harnessing the evolved bacteria as cystine-addicted living biocatalyst for antitumor metabolic therapy
GEO Series GSE260605. Escherichia coli. 6 samples. Type: Expression profiling by high throughput sequencing.
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