Purification and characterization of plant fructan:fructan fructosyltransferases
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1 Research Collection Doctoral Thesis Purification and characterization of plant fructan:fructan fructosyltransferases Author(s): Lüscher, Marcel Publication Date: 1992 Permanent Link: Rights / License: In Copyright - Non-Commercial Use Permitted This page was generated automatically upon download from the ETH Zurich Research Collection. For more information please consult the Terms of use. ETH Library
2 Diss. ETH No 9938 Purification and characterization of plant fructamfructan fructosyltransf erases a dissertation submitted to the SWISS FEDERAL INSTITUTE OF TECHNOLOGY, ZÜRICH for the degree of Doctor in Natural Science by Marcel Liischer Dipl. Natw. ETH born January 21st, 1962 citizen of Muhen (AG) Accepted on the recommendation of Prof. Dr. J. Nosberger, examiner P«Ar^»/-<-^^_^ Dr. M. Frehner, co-examiner Prof. Dr. N. Amrhein, co-examiner Zürich, 1992
3 1 1. Summary Fructans are direct parameters of the yield stability of many agricultural crops. In order to elucidate fructan metabolism, we purified fructan:fructan fructosyltransferases (FFT, EC ) from three different plants. This enzyme is assumed to perform fructan chain elongation in plants. The purification to homogeneity of FFTs from two members of the Compositae {Helianthus tuberosus L. and Taraxacum officinale Weber) is reported here for the first time. Thus the model for fructan metabolism of Edelman & Jefford (1968) appears to retain its validity even under the severe scrutiny of modem biochemical purification procedures. In barley, FFT, SST and sugar degrading activities were partially separated; therefore, it is suggested that a similar model for fructan metabolism applies to barley. The FFT from Helianthus tuberosus was isolated by a four step purification procedure. This protein preparation was separated into three bands by sodium dodecylsulfate Polyacrylamide gel electrophoresis (SDS PAGE) and into eight forms by iso-electric focusing (IEF). These forms were partially purified and FFT activity was detected in all the fractions. Six of these proteins had the same apparent MW of 72.8 kd by SDS PAGE, while two of them were smaller (60.5 and 56.2 kd). The enzyme was most active at ph 6.5. After pre incubation (1 h) at temperatures of up to 40 C. the residual FFT activity was > 80%. FFT transferred fructosyl groups from oligofructans (degree of polymerization (DP) 3 to 8) of the inulin series. No glycosyl transfer occurred with 6-kestose, neokestose, maltose, raffinose and maltotriose as the sole substrate. Sucrose efficiently accepted fructosyl units from oligofructans with a Km of approximately 0.2 mm. The FFT of another member of the Compositae, Taraxacum officinale, was purified. After a five step purification procedure, separation of proteins by SDS PAGE yielded two bands with molecular weights of 60.5 and 56.2 kd. The smaller protein was obtained by ion exchange chromatography and contained FFT activity. The ph optimum, temperature stability and substrate specificity of the dandelion FFT were almost identical to those of H. tuberosus. Thus, the FFTs of the Compositae family may be closely related. FFT activity was highly purified from barley primary biosynthesis. Fructosyl transferases and sugar degrading leaves induced for fructan activities were well separated, but even after high resolution purification techniques (IEF), the FFT activity was not completely resolved from sugar degrading activities. The ability to partially separate the three activities (FFT, SST and sugar
4 2 degrading activities) indicates that similar enzymes to those in Edelman & Jefford's model for fructan biosynthesis in H. tuberosus exist in barley. However, neither the model activities nor the purified barley FFT account for the structural diversity of barley fructan. In a different approach several grass cell suspension cultures were established. A culture of Phleum pratense L. produced fructans, and could be induced to accumulate even more by cold treatment. However, as an experimental system for protein purification this culture was unsuitable because of its slow growth rate, the long induction time required amount of FFT activity detectable. and the low
5 3 3. Zusammenfassung Fruktane können wichtige Parameter der Ertragsstabilität darstellen. Einblicke in die Enzymologie der Fruktanbiosynthese sind wichtig zum Verständnis ertragsphysiologischer Prozesse bei Getreidearten und Gräsern des gemässigten Klimas. Um die Fruktanbiosynthese zu untersuchen und deren Mechanismen genauer zu verstehen, wurden Fruktan:fruktan fruktosyltransferasen (FFT, EC ) von drei verschiedenen Pflanzen gereinigt und charakterisiert. Die FFT gilt als kettenverlängerndes Enzym der Fruktanbiosynthese. Die vollständige Reinigung von FFTs aus zwei Kompositen (Helianthus tuberosus L., Taraxacum officinale Weber) wurde hier zum ersten Mal durchgeführt. Damit konnte die FFT im Modell von Edelman & Jefford (1968) in Bezug auf die Fruktankettenverlängerung experimentell nachgewiesen werden. In Gerste konnten Enzymaktivitäten wie Saccharose:saccharose fruktosyltransferase (SST), FFT und Exohydrolasen partiell gereinigt werden. Dieses Resultat bestätigt die Vermutung, dass, abgesehen von der strukturellen Vielfalt der Fruktane, die Fruktanbiosynthese in Gerste ähnlich wie im Modell von Edelman & Jefford abläuft. In vier Reinigungsschritten wurde die FFT von Helianthus tuberosus L. bis auf drei Banden nach Natriumdodecylsulphat-Polyacrylamid- Gelelektrophorese (SDS-PAGE) gereinigt. Diese Proteine konnten mit isoelektrischer Focusierung (IEF) in acht Formen aufgetrennt werden. Der isoelektrische Punkt dieser Proteine lag im ph-bereich von 4.3 und 4.5. Mit präparativer IEF wurden die acht Formen partiell aufgetrennt und in all diesen Fraktionen konnte FFT-Aktivität nachgewiesen werden. Sechs der Formen wiesen dasselbe Molekulargewicht (MW) von 72.8 kd auf, während zwei davon kleiner waren (60.5 und 56.2 kd). Das Enzymgemisch hatte ein ph-optimum bei ph 6.5 und nach Vorinkubation (1h) bis zu 40 C konnte noch über 80% der Aktivität nachgewiesen werden. Die gereinigte FFT transferierte Fruktosylgruppen von Oligofruktanen (Polymerisierungsgrad (DP) 3 bis 8) der Inulinserie. Kein Glykosyltransfer konnte nachgewiesen werden mit 6-Kestose, Neokestose, Maltose und Raffinose als Substrat. Saccharose war ein effizienter Fruktosylakzeptor nicht aber Fruktosyldonor. Der Km-Wert für Saccharose als Akzeptor betrug 0.2 mm. Damit die FFT von H. tuberosus mit jener einer anderen Komposite verglichen werden konnte, wurde die FFT von Taraxacum officinale gereinigt. In fünf Reinigungsschritten wurde die FFT bis auf zwei Banden nach SDS-PAGE gereinigt. Das MW der
6 4 beiden Banden betrug 60.5 bzw 56.2 kd. Das kleinere Protein konnte isoliert und FFT-Aktivität nachgewiesen werden. Die FFT zeigte dieselbe Temparaturstabilität und dasselbe ph-optimum wie jene von H.tuberosus sowie eine sehr ähnliche Substratspezifität. Dies könnte darauf hinweisen, dass die FFTs unter Kompositen stark verwandt sind. Die FFT aus lichtinduzierten Gerstenblättern wurde hoch gereinigt. Die Fruktosyltransferasen wie auch die zuckerabbauenden Aktivitäten konnten weitgehend getrennt werden. Doch selbst mit hochauflösenden Reinigungstechniken (IEF) konnte die FFT nicht gänzlich von den zuckerabbauenden Enzymaktivitäten getrennt werden. Die Möglichkeit der partiellen Trennung von den drei Enzymaktivitäten (SST, FFT und zuckerabbauende Enzyme) weist darauf hin, dass ähnliche Enzymmuster wie in H.tuberosus für die Fruktanbiosynthese in Gerste vorkommen könnten. Verschiedene Graszellkulturen wurden mit dem Ziel etabliert, diese als experimentelle Modelle zur Untersuchung der Fruktanbiosynthese zu verwenden. Eine Kultur von Phleum pratense akkumulierte Fruktane intrazellulär und durch Kälteinduktion konnte eine Erhöhung der Fruktannettoproduktion erzielt werden. Als experimentelles System für die Enzymreinigung war diese Kultur jedoch ungeeignet, da trotz Induzierbarkeit, nur sehr kleine FFT-Aktivitäten in vitro nachzuweisen waren.
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