Hot or not? Discovery and characterization of a thermostable alditol oxidase from Acidothermus cellulolyticus 11B View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2012-07

AUTHORS

Remko T. Winter, Dominic P. H. M. Heuts, Egon M. A. Rijpkema, Edwin van Bloois, Hein J. Wijma, Marco W. Fraaije

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. More... »

PAGES

389-403

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00253-011-3750-0

DOI

http://dx.doi.org/10.1007/s00253-011-3750-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020270064

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/22231860


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