Molecular characterization and expression of a novel alcohol oxidase from Aspergillus terreus MTCC6324.
Mitun Chakraborty,Manish Goel,Somasekhar R. Chinnadayyala,Ujjwal Ranjan Dahiya,Siddhartha Sankar Ghosh,Pranab Goswami +5 more
TL;DR: The deduced amino acid sequences of recombinant rAOx showed maximum structural homology with the chain B of aryl AOx from Pleurotus eryngii, and docking studies with an ab-initio protein model demonstrated the presence of a conserved FAD binding domain with an active substrate binding site.
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Abstract: The alcohol oxidase (AOx) cDNA from Aspergillus terreus MTCC6324 with an open reading frame (ORF) of 2001 bp was constructed from n-hexadecane induced cells and expressed in Escherichia coli with a yield of ∼4.2 mg protein g−1 wet cell. The deduced amino acid sequences of recombinant rAOx showed maximum structural homology with the chain B of aryl AOx from Pleurotus eryngii. A functionally active AOx was achieved by incubating the apo-AOx with flavin adenine dinucleotide (FAD) for ∼80 h at 16°C and pH 9.0. The isoelectric point and mass of the apo-AOx were found to be 6.5±0.1 and ∼74 kDa, respectively. Circular dichroism data of the rAOx confirmed its ordered structure. Docking studies with an ab-initio protein model demonstrated the presence of a conserved FAD binding domain with an active substrate binding site. The rAOx was specific for aryl alcohols and the order of its substrate preference was 4-methoxybenzyl alcohol >3-methoxybenzyl alcohol>3, 4-dimethoxybenzyl alcohol > benzyl alcohol. A significantly high aggregation to ∼1000 nm (diameter) and catalytic efficiency (kcat/Km) of 7829.5 min−1 mM−1 for 4-methoxybenzyl alcohol was also demonstrated for rAOx. The results infer the novelty of the AOx and its potential biocatalytic application.
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Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.
TL;DR: Different lignocellulolytic redox systems, enzymatic or not, that depend on fluxes of reactive oxygen species (ROS) are presented and it is suggested that fine-tuning of H2O2 levels and proximity between sites of H1O2 production and consumption are important for fungal biomass conversion.
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The GMC superfamily of oxidoreductases revisited: analysis and evolution of fungal GMC oxidoreductases
TL;DR: This study offers new insights into the sequence variation and phylogenetic relationships of fungal GMC/AA3 sequences and interpret the results from an evolutionary perspective, where it could show, for example, that pyranose dehydrogenase evolved from aryl-alcohol oxidoreductase after a change in substrate specificity and that the cytochrome domain of cellobiose dehydrogensase was regularly lost during evolution.
Pecularities and applications of aryl-alcohol oxidases from fungi
TL;DR: Aryl-Alcohol oxidases (AAOs) are FAD-containing enzymes that oxidize a broad range of aromatic as well as aliphatic allylic alcohols to aldehydes as discussed by the authors.
Highly Active and Stable Large Catalase Isolated from a Hydrocarbon Degrading Aspergillus terreus MTCC 6324
Preety Vatsyayan,Pranab Goswami +1 more
TL;DR: The catalytic efficiency and alkaline pH stability of the Aspergillus terreus MTCC 6324 large catalase (CAT) are considerably higher than most of the extensively studied catalases from different sources.
Reaction mechanisms and applications of aryl-alcohol oxidase
TL;DR: Aryl-alcohol oxidases constitute a family of FAD-containing enzymes, included in the glucose-methanol-choline oxidase/dehydrogenase superfamily of proteins, and can be used for different biotechnological applications, such as flavor synthesis, secondary alcohol deracemization and oxidation of furfurals for the production of furandicarboxylic acid as a chemical building block.
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