Purification and some properties of fructan: fructan fructosyl transferase from dandelion (Taraxacum officinale Weber)

Abstract

A fructan: fructan fructosyl transferase (FFT, EC 2.4.1.100) was purified 61‐4‐fold from roots of Taraxacum officinale Weber. The enzyme is a glycoprotein with an apparent molecular weight of 49000 as determined by SDS‐polyacrylamide gel electrophoresis. FFT activity was detected by 1‐kestose‐dependent nystose production. The enzyme was most active at pH 6·5 and was stable at 30°C (1 h). Separation by preparative iso‐electric focusing yielded four different forms with iso‐electric points around pH 4·8. The purified enzyme was active on different oligofructans of the inulin series, but not on melezitose, 6‐kestose, neokestose, maltopentaose or sucrose as the sole substrate. Copyright © 1993, Wiley Blackwell. All rights reserved