Expression and characterization of α-1,3-glucanase from Paenibacillus alginolyticus NBRC15375, which is classified into subgroup 2 (minor group) of GH family 87

Biosci Biotechnol Biochem. 2024 Apr 22;88(5):538-545. doi: 10.1093/bbb/zbae014.

Abstract

Bacterial α-1,3-glucanase, classified as glycoside hydrolase (GH) family 87, has been divided into 3 subgroups based on differences in gene sequences in the catalytic domain. The enzymatic properties of subgroups 1 and 3 of several bacteria have been previously investigated and reported; however, the chemical characterization of subgroup 2 enzymes has not been previously conducted. The α-1,3-glucanase gene from Paenibacillus alginolyticus NBRC15375 (PaAgl) belonging to subgroup 2 of GH family 87 was cloned and expressed in Escherichia coli. PgAgl-N1 (subgroup 3) and PgAgl-N2 (subgroup 1) from P. glycanilyticus NBRC16188 were expressed in E. coli, and their enzymatic characteristics were compared. The amino acid sequence of PaAgl demonstrated that the homology was significantly lower in other subgroups when only the catalytic domain was compared. The oligosaccharide products of the mutan-degrading reaction seemed to have different characteristics among subgroups 1, 2, and 3 in GH family 87.

Keywords: Paenibacillus alginolyticus; Paenibacillus glycanilyticus; expression; subgroup of bacterial α-1,3-glucanase.

MeSH terms

  • Amino Acid Sequence*
  • Catalytic Domain
  • Cloning, Molecular*
  • Escherichia coli* / genetics
  • Gene Expression*
  • Glycoside Hydrolases* / chemistry
  • Glycoside Hydrolases* / genetics
  • Glycoside Hydrolases* / metabolism
  • Hydrogen-Ion Concentration
  • Oligosaccharides / metabolism
  • Paenibacillus* / enzymology
  • Paenibacillus* / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Substrate Specificity

Substances

  • Glycoside Hydrolases
  • Recombinant Proteins
  • exo-1,3-alpha-glucanase
  • Oligosaccharides