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Purification and some properties of fructan: fructan fructosyl transferase from dandelion ( Taraxacum officinale Weber)
Author(s) -
LÜSCHER M.,
FREHNER M.,
NÖSBERGER J.
Publication year - 1993
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.1993.tb03755.x
Subject(s) - fructan , dandelion , taraxacum officinale , inulin , transferase , chemistry , chromatography , sucrose , enzyme , substrate (aquarium) , biochemistry , biology , medicine , ecology , alternative medicine , traditional chinese medicine , pathology
SUMMARY 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.