Partial Purification and Characterization of UDP-Glucose: Salicyl Alcohol Glucosyltransferase from Gardenia jasminoides Cell Cultures

Abstract

A new enzyme, UDP-glucose: salicyl alcohol glucosyltransferase, was purified 110-fold from Gardenia jasminoides cell cultures. The enzyme catalyzes position-specific glucosylation of salicyl alcohol to form salicin using UDP-glucose as a glucose donor. The molecular weight of the enzyme as estimated by gel filtration is 51,000. Apparent Km values for salicyl alcohol and UDP-glucose are 0.11 and 0.031 mM, respectively. The enzyme shows a pH optimum between 9.0 and 9.5. Sulfhydryl inhibitors and some divalent cations inhibit the enzyme activity. The glucosyltransferase exhibits a strict substrate specificity for salicyl alcohol.