Acceptor specificity of cyclodextrin glycosyltransferase from Bacillus stearothermophilus and synthesis of alpha-D-glucosyl O-beta-D-galactosyl-(1----4)-beta-D-glucoside

Biosci Biotechnol Biochem. 1992 Sep;56(9):1386-91. doi: 10.1271/bbb.56.1386.

Abstract

Bacillus stearothermophilus CGTase had a wider acceptor specificity than Bacillus macerans CGTase did and produced large amounts of transfer products of various acceptors such as D-galactose, D-mannose, D-fructose, D- and L-arabinose, D- and L-fucose, L-rhamnose, D-glucosamine, and lactose, which were inefficient acceptors for B. macerans CGTase. The main component of the smallest transfer products of lactose was assumed to be alpha-D-glucosyl O-beta-D-galactosyl-(1----4)-beta-D-glucoside.

Publication types

  • Comparative Study

MeSH terms

  • Bacillus / enzymology
  • Carbohydrate Sequence
  • Chromatography, High Pressure Liquid
  • Geobacillus stearothermophilus / enzymology*
  • Glucosyltransferases / metabolism*
  • Lactose / metabolism
  • Molecular Sequence Data
  • Monosaccharides / metabolism
  • Starch / metabolism
  • Substrate Specificity
  • Trisaccharides / metabolism*

Substances

  • Monosaccharides
  • Trisaccharides
  • glucosyl-O-galactosyl-(1-4)glucoside
  • Starch
  • Glucosyltransferases
  • cyclomaltodextrin glucanotransferase
  • Lactose