Isolation and characterization of a novel GH67 α-glucuronidase from a mixed culture

J Ind Microbiol Biotechnol. 2012 Aug;39(8):1245-51. doi: 10.1007/s10295-012-1128-7. Epub 2012 Apr 24.

Abstract

Hemicelluloses represent a large reservoir of carbohydrates that can be utilized for renewable products. Hydrolysis of hemicellulose into simple sugars is inhibited by its various chemical substituents. The glucuronic acid substituent is removed by the enzyme α-glucuronidase. A gene (deg75-AG) encoding a putative α-glucuronidase enzyme was isolated from a culture of mixed compost microorganisms. The gene was subcloned into a prokaryotic vector, and the enzyme was overexpressed and biochemically characterized. The DEG75-AG enzyme had optimum activity at 45 °C. Unlike other α-glucuronidases, the DEG75-AG had a more basic pH optimum of 7-8. When birchwood xylan was used as substrate, the addition of DEG75-AG increased hydrolysis twofold relative to xylanase alone.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Endo-1,4-beta Xylanases / metabolism
  • Escherichia coli
  • Glucuronic Acid / metabolism
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / isolation & purification*
  • Glycoside Hydrolases / metabolism*
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Molecular Sequence Data
  • Polysaccharides / metabolism
  • Soil Microbiology*
  • Temperature
  • Xylans / metabolism

Substances

  • Polysaccharides
  • Xylans
  • hemicellulose
  • Glucuronic Acid
  • Glycoside Hydrolases
  • alpha-glucuronidase
  • Endo-1,4-beta Xylanases