Enzymatic synthesis of puerarin glucosides using Leuconostoc Dextransucrase

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 α-D-glucosyl- (1→6)-P (P-G) by using LC-MS or 1H- or 13C-NMR spectroscopies and α-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. © The Korean Society for Microbiology and Biotechnology.