Skip to main content
Article
Flavanone-specific O-7 glucosyltransferase activity in Citrus paradisi seedlings: Purification and characterization.
Archives of Biochemistry and Biophysics (1990)
  • Cecilia A. McIntosh, East Tennessee State University
  • Lilian Latchinian, Concordia University, Montreal, Quebec, Canada
  • Richard L. Mansell, University of South Florida
Abstract
The isolation and characterization of a flavanonespeciflc 7-O-glucosyltransferase and its resolution from other glucosyltransferases in Citrus paradisi (grapefruit) seedlings is described. This new enzyme in the subclass 2.4.1 catalyzes the glucosylation of the 7-OH group of naringenin (4′,5′,7-trihydroxyflavanone) to prunin and has been purified (943-fold) by fractional precipitation with ammonium sulfate and successive chromatography on Sephadex G-100, hydroxyapatite, UDP-glucuronic acid agarose, Mono Q, and Mono P columns. It has a pH optimum of 7.5–8.0, an apparent pI of 4.3, and an apparent Mr of 54,900. This glucosyltransferase has an expressed specificity for the 7-position of the flavanones naringenin (Kmapp 62 μm; Kmapp UDPG 51 μm) and hesperetin (Kmapp 124 μm; Kmapp UDPG 243 μm) and did not accept other flavone or flavonol aglycones. Characteristics of other flavonoid glucosyltransferase activities found in grapefruit seedlings are also described.
Publication Date
October 1, 1990
DOI
10.1016/0003-9861(90)90085-D
Citation Information
McIntosh, C. A., Latchinian, L., & Mansell, R. L. (1990). Flavanone-specific 7-O-glucosyltransferase activity in Citrus paradisi seedlings: Purification and characterization. Archives of Biochemistry and Biophysics, 282(1), 50–57. https://doi.org/10.1016/0003-9861(90)90085-D