Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis

Int J Biol Macromol. 2015 Aug:79:72-5. doi: 10.1016/j.ijbiomac.2015.04.054. Epub 2015 Apr 30.

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are recently discovered oxidative enzymes that are capable of oxidative cleavage of recalcitrant polysaccharides such as chitin or cellulose. Despite the importance of LPMOs in biomass conversion and the large number of lpmo genes in microorganisms, only a few LPMOs have been well studied, and further characterization of these proteins is thus of interest. In this study, a chitin-active AA10 family LPMO from Bacillus thuringiensis subsp. kurstaki, BtLPMO10A, is described. This enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin, however, interestingly, when colloidal chitin is used as the substrate, a ladder of oxidized oligosaccharides is observed. These results provide new insights into the action mode of LPMOs that may be affected by the substrates.

Keywords: B. thuringiensis; Lytic polysaccharide monooxygenases; Polysaccharides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus thuringiensis / chemistry*
  • Bacillus thuringiensis / enzymology
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Catalytic Domain
  • Chitin / chemistry*
  • Cloning, Molecular
  • Colloids
  • Crystallization
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Hydrolysis
  • Mixed Function Oxygenases / chemistry*
  • Mixed Function Oxygenases / genetics
  • Oligosaccharides / chemistry*
  • Oxidation-Reduction
  • Protein Binding
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Colloids
  • Oligosaccharides
  • Recombinant Proteins
  • Chitin
  • Mixed Function Oxygenases