ArticlePloS one2014
Molecular characterization and expression of a novel alcohol oxidase from Aspergillus terreus MTCC6324.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Plant Biomass Depolymerization by Oxidoreductases: Structural Characteristics, Synergy Mechanism, and Evolutionary Adaptation.Journal of agricultural and food chemistry · 2026Review
- Aryl-alcohol oxidases: catalysis, diversity, structure-function and emerging biotechnological applications.Applied microbiology and biotechnology · 2025Review
- Structure-Guided Evolution Modulate Alcohol Oxidase to Improve Ethanol Oxidation Performance.Applied biochemistry and biotechnology · 2024Article
- Unveiling the kinetic versatility of aryl-alcohol oxidases with different electron acceptors.Frontiers in bioengineering and biotechnology · 2024Article
- A broadly conserved fungal alcohol oxidase (AOX) facilitates fungal invasion of plants.Molecular plant pathology · 2023Article
- Oxidation of 5-hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601.Microbial biotechnology · 2022Article
- The GMC superfamily of oxidoreductases revisited: analysis and evolution of fungal GMC oxidoreductases.Biotechnology for biofuels · 2019Article
- Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.Microbiology and molecular biology reviews : MMBR · 2018Review
- Highly Active and Stable Large Catalase Isolated from a Hydrocarbon Degrading Aspergillus terreus MTCC 6324.Enzyme research · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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