Enzymatic synthesis of puerarin glucosides using Leuconostoc dextransucrase

J Microbiol Biotechnol. 2012 Sep;22(9):1224-9. doi: 10.4014/jmb.1202.02007.

Abstract

Puerarin (P), an isoflavone derived from kudzu roots, has strong biological activities, but its bioavailability is often limited by its low water solubility. To increase its solubility, P was glucosylated by three dextransucrases from Leuconostoc or Streptococcus species. Leuconostoc lactis EG001 dextransucrase exhibited the highest productivity of puerarin glucosides (P-Gs) among the three tested enzymes, and it primarily produced two P-Gs with a 53% yield. Their structures were identified as alpha-D-glucosyl-(1-->6)-P (P-G) by using LC-MS or (1)H- or (13)C-NMR spectroscopies and alpha-D-isomaltosyl-(1-->6)-P (P-IG2) by using specific enzymatic hydrolysis, and their solubilities were 15- and 202-fold higher than that of P, respectively. P-G and P-IG2 are easily applicable in the food and pharmaceutical industries as alternative functional materials.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Glucosides / biosynthesis*
  • Glucosides / chemistry
  • Glucosyltransferases / chemistry
  • Glucosyltransferases / genetics
  • Glucosyltransferases / isolation & purification
  • Glucosyltransferases / metabolism*
  • Glycosylation
  • Isoflavones / biosynthesis*
  • Isoflavones / chemistry
  • Leuconostoc / enzymology*
  • Leuconostoc / genetics
  • Solubility

Substances

  • Bacterial Proteins
  • Glucosides
  • Isoflavones
  • Glucosyltransferases
  • dextransucrase
  • puerarin