ArticleApplied microbiology and biotechnology2012
Hot or not? Discovery and characterization of a thermostable alditol oxidase from Acidothermus cellulolyticus 11B.
Article in Applied microbiology and biotechnology, 2012. 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, 29 citations in OpenAlex.
- Biogeographical Distribution of Bacteria in Soils with Identical Agricultural Practices: Impacts of Environmental Factors.Current microbiology · 2025Article
- Discovery and biochemical characterization of thermostable glycerol oxidases.Applied microbiology and biotechnology · 2024Article
- Strategies for the synthesis of the osmolyte glucosylglycerate and its precursor glycerate.Applied microbiology and biotechnology · 2024Review
- Highly Efficient Synthesis of Rare Sugars from Glycerol in Endotoxin-FreeFoods (Basel, Switzerland) · 2023Article
- Directed evolution of alditol oxidase for the production of optically pure D-glycerate from glycerol in the engineered Escherichia coli.Journal of industrial microbiology & biotechnology · 2021Article
- Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase.Angewandte Chemie (International ed. in English) · 2020Article
- Creating Oxidase-Peroxidase Fusion Enzymes as a Toolbox for Cascade Reactions.Chembiochem : a European journal of chemical biology · 2017Article
- The substrate tolerance of alcohol oxidases.Applied microbiology and biotechnology · 2015Review
- Thermophilic and alkaliphilic Actinobacteria: biology and potential applications.Frontiers in microbiology · 2015Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe the discovery, isolation and characterization of a highly thermostable alditol oxidase from Acidothermus cellulolyticus 11B. This protein was identified by searching the genomes of known thermophiles for enzymes homologous to Streptomyces coelicolor A3(2) alditol oxidase (AldO). A gene (sharing 48% protein sequence identity to AldO) was identified, cloned and expressed in Escherichia coli. Following 6xHis tag purification, characterization revealed the protein to be a covalent flavoprotein of 47 kDa with a remarkably similar reactivity and substrate specificity to that of AldO. A steady-state kinetic analysis with a number of different polyol substrates revealed lower catalytic rates but slightly altered substrate specificity when compared to AldO. Thermostability measurements revealed that the novel AldO is a highly thermostable enzyme with an unfolding temperature of 84 °C and an activity half-life at 75 °C of 112 min, prompting the name HotAldO. Inspired by earlier studies, we attempted a straightforward, exploratory approach to improve the thermostability of AldO by replacing residues with high B-factors with corresponding residues from HotAldO. None of these mutations resulted in a more thermostable oxidase; a fact that was corroborated by in silico analysis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.