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First published online January 9, 2003; 10.1104/pp.015305

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Plant Physiol, February 2003, Vol. 131, pp. 621-631

Fructan 1-Exohydrolases. beta -(2,1)-Trimmers during Graminan Biosynthesis in Stems of Wheat? Purification, Characterization, Mass Mapping, and Cloning of Two Fructan 1-Exohydrolase Isoforms1,[w]

Wim Van den Ende,* Stefan Clerens, Rudy Vergauwen, Liesbet Van Riet, André Van Laere, Midori Yoshida, and Akira Kawakami

Department of Biology, Laboratory for Developmental Biology, Botany Institute, KULeuven, Kasteelpark Arenberg 31, B-3001 Leuven, Belgium (W.V.d.E., R.V., L.V.R., A.V.L.); Department of Biology, Laboratory of Neuro-endocrinology and Immunological Biotechnology, Zoological Institute, KULeuven, Naamsestraat 59, B-3000 Leuven, Belgium (S.C.); and National Agricultural Research Centre for Hokkaido Region, Hitsujigaoka, Sapporo 062-8555, Japan (M.Y., A.K.)

Graminan-type fructans are temporarily stored in wheat (Triticum aestivum) stems. Two phases can be distinguished: a phase of fructan biosynthesis (green stems) followed by a breakdown phase (stems turning yellow). So far, no plant fructan exohydrolase enzymes have been cloned from a monocotyledonous species. Here, we report on the cloning, purification, and characterization of two fructan 1-exohydrolase cDNAs (1-FEH w1 and w2) from winter wheat stems. Similar to dicot plant 1-FEHs, they are derived from a special group within the cell wall-type invertases characterized by their low isoelectric points. The corresponding isoenzymes were purified to electrophoretic homogeneity, and their mass spectra were determined by quadrupole-time-of-flight mass spectrometry. Characterization of the purified enzymes revealed that inulin-type fructans [beta -(2,1)] are much better substrates than levan-type fructans [beta -(2,6)]. Although both enzymes are highly identical (98% identity), they showed different substrate specificity toward branched wheat stem fructans. Although 1-FEH activities were found to be considerably higher during the fructan breakdown phase, it was possible to purify substantial amounts of 1-FEH w2 from young, fructan biosynthesizing wheat stems, suggesting that this isoenzyme might play a role as a beta -(2,1)-trimmer throughout the period of active graminan biosynthesis. In this way, the species and developmental stage-specific complex fructan patterns found in monocots might be determined by the relative proportions and specificities of both fructan biosynthetic and breakdown enzymes.

1 This work was supported by the Fund for Scientific Research Flanders. W.V.d.E. is a Postdoc supported by the Fund for Scientific Research Flanders.

* Corresponding author; e-mail wim.vandenende{at}bio.kuleuven.ac.be; fax 32-16-321967.

[w]  The online version of this article contains Web-only data. The supplemental material is available at www.plantphysiol.org.

© 2003 American Society of Plant Biologists


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