Journal of Microbiology and Biotechnology 2012-09-01

Enzymatic synthesis of puerarin glucosides using Leuconostoc dextransucrase.

Jin-A Ko, Young Bae Ryu, Tae-Soon Park, Hyung Jae Jeong, Jang-Hoon Kim, Su-Jin Park, Joong-Su Kim, Doman Kim, Young-Min Kim, Woo Song Lee

Index: J. Microbiol. Biotechnol. 22(9) , 1224-9, (2012)

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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.

Related Compounds

  • Dextran sucrase

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