Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48

Biosci Biotechnol Biochem. 1996 Apr;60(4):640-4. doi: 10.1271/bbb.60.640.


A novel enzyme, trehalose synthase, was purified from a cell-free extract of Pimelobacter sp. R48 to an electrophoretically homogeneous state by successive chromatographies on DEAE-Toyopearl 650, Butyl-Toyopearl 650, and Mono Q HR5/5 columns. The molecular weight of the enzyme was estimated to be 62,000 by SDS-polyacrylamide gel electrophoresis, and the enzyme had a pI of 4.6 by gel isoelectrofocusing. The enzyme catalyzed the conversion of maltose into trehalose by intramolecular transglucosylation. The enzyme also converted into maltose but was inactive on other saccharides. The N-terminal amino acid of the enzyme was serine. The optimum pH and temperature were pH7.5 and 20 degrees C, respectively. The enzyme was stable in the range of pH 6.0-9.0 and up to 30 degrees C for 60 min. The rate of conversion of maltose into trehalose was independent of the maltose concentration. The maximum yield of trehalose from maltose were 81.8%, 80.9%, and 76.7% at 5, 15, and 25 degrees C, respectively. The activity was inhibited by Cu2+, Hg2+, Ni2+, Zn2+, and Tris.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Glucosyltransferases / chemistry
  • Glucosyltransferases / isolation & purification*
  • Glycosylation
  • Gram-Positive Asporogenous Rods / genetics*
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Molecular Weight
  • Substrate Specificity
  • Temperature


  • Amino Acids
  • Glucosyltransferases
  • trehalose synthase