Glycosylation of various flavonoids by recombinant oleandomycin glycosyltransferase from Streptomyces antibioticus in batch and repeated batch modes

Biotechnol Lett. 2012 Mar;34(3):499-505. doi: 10.1007/s10529-011-0789-z. Epub 2011 Nov 25.

Abstract

An oleandomycin glycosyltransferase (OleD GT) gene from Streptomyces antibioticus was functionally expressed in Escherichia coli BL21 (DE3) with various molecular chaperones. The purified recombinant OleD GT catalyzed glycosylation of various flavonoids: apigenin, chrysin, daidzein, genistein, kaempferol, luteolin, 4-methylumbelliferone, naringenin, quercetin and resveratrol with UDP-glucose. 4.6 μg OleD GT was readily immobilized onto 1 mg hybrid nanoparticles of Fe(3)O(4)/silica/NiO on the basis of the affinity between His-tag and NiO nanoparticles with retention of 90% activity. In batch reaction, more than 90% naringenin (20 μM) was converted to its glycoside in 5 h. The immobilized OleD GT was efficiently reused for seven times whilst maintaining >60% of the residual activity in repeated glycosylation of naringenin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzymes, Immobilized / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Flavonoids / metabolism*
  • Gene Expression
  • Glycosylation
  • Glycosyltransferases / isolation & purification
  • Glycosyltransferases / metabolism*
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Streptomyces antibioticus / enzymology*
  • Streptomyces antibioticus / genetics
  • Uridine Diphosphate Glucose / metabolism

Substances

  • Enzymes, Immobilized
  • Flavonoids
  • Recombinant Proteins
  • Glycosyltransferases
  • Uridine Diphosphate Glucose