New features of plant-fructan structure revealed by methylation analysis and carbon-13 n.m.r. spectroscopy

Carpita, Nicholas C.; Housley, T. L.; Hendrix, John E.

doi:10.1016/0008-6215(91)84123-v

Cited by 59 publications

(35 citation statements)

References 26 publications

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“…Phleins, i.e. p 2-6-linked polymers, are present only in traces in the low-DP fructan pool (Spollen and Nelson, 1988), but the hig'h-DP pool contains a high ratio of 2-6-linked fructans (Carpita et al, '1991). Our enzyme preparations synthesized fructan with a pattern identical with those of the low-DP pool.…”

Section: Table I Effect Of Protein Purification On Relative Activitiesmentioning

confidence: 80%

Fructosyltransferase Activities in the Leaf Growth Zone of Tall Fescue

Lüscher

Nelson

1995

Plant Physiol.

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High concentrations of water-soluble carbohydrates, mainly fructan, accumulate in the growth zone of tal1 fescue (Festuca arundinacea Schreb.) leaf blades. We studied sucrose-hydrolyzing activities in the leaf growth zone because of their importance in carbohydrate partitioning. Sucrose hydrolysis in the basal 1.5 cm was largely due to fructosyltransferases, which had activities up to 10 times higher than in fully developed leaf tissue. Three fructosyltransferases (Fl, F2, and F3) were purified from the leaf growth zone. Each synthesized, from either sucrose or 1-kestose, a mixture of trisaccharides and higher-order oligofructans identical with the low-degree of polymerization fructan extracted from similar plant tissue. The highly purified fructosyltransferases retained ability (1 3%) to transfer fructose from sucrose to water. Time-dependent and substrate-dependent studies, using sucrose as the substrate, showed proportional production of fructose and glucose, indicating that both products are from the same enzyme. Fructosyltransferase was calculated to contribute about half the total transfer of fructose to water in the basal 1.5 cm. lnvertase activity increased to near 2.0 cm when fructosyl transfer to sucrose and other oligofructans decreased. lnvertase was the major activity for sucrose hydrolysis at positions dista1 to 3.0 cm.

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Section: Table I Effect Of Protein Purification On Relative Activitiesmentioning

confidence: 80%

Fructosyltransferase Activities in the Leaf Growth Zone of Tall Fescue

Lüscher

Nelson

1995

Plant Physiol.

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“…Hence, steric hindrance of the hydrolytic reaction due to the branch point was not apparent, which might distinguish the FEH preferring //-(2-6)-fructose linkages from the /3-{2-l)-specific FEH. Indeed, our 6-FEH hydrolysed a mixture of branched and predominantly yS-(2-6)-linked oligofructans of DP > 7 from Triticum (Mature Stems in Table 1 in Carpita, Housley & Hendrix, 1991;Bancal & TriboT, 1993) reasonably well. The fructan mixture was used at about 30% of the concentration of 6,6-kestotetraose (by mass); however, the relative acti^'ity was 40 % of that with 6,6-kestotetraose.…”

Section: Substrates Of 6-fehmentioning

confidence: 80%

Hydrolysis of fructan in grasses: a β‐(2‐6)‐linkage specific fructan‐β‐fructosidase from stubble of Lolium perenne

1997

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SUMMARYSeveral different fructan and sucrose hydrolysing enzyme activities were induced in roots and stubble (mainly leaf sheaths) of Lolium perenne L. plants after defoliation. Among those activities, a fructan-/?-fructosidase (EC 3 .2.1.80) that hydrolyses predominantly /?-(2-6)-fructosyl-fructose linkages (6-FEH) was purified from the stubble. The use of the substrate 6,6-kestotetraose and high-performance anion-exchange chromatography with pulsed amperometric detection allowed linkage-specific screening and sensitive analysis of enzyme activity. A 6-FEH was extensively purified to yield one protein band as revealed by one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The 6-FEH was separated from the contaminating y9.(2-l)-linkage-specific fructan-/9-fructosidase and invertase activities (EC 3.1.2.26) by ammonium sulphate precipitation, lectin-affinity, anion-exchange and size-exclusion chromatography. The purified 6-FEH was a glycoprotein with an apparent molecular mass of 65000, as determined by size-exclusion chromatography, and of 69000 by SDS-PAGE. The 6-FEH had an activity optimum in the range of pH 5-1 to 5-6. Temperatures above 30 °C affected the stability of the enzyme activity; however, its temperature stability was increased in the presence of 6,6-kestotetraose. The purified 6-FEH activity hydrolysed the/ff-(2-6)-linkages in 6,6-kestotetraose and (1&6)-kestotetraose at rates five times faster than the /?-(2-l)-linkages in 1,1-kestotetraose and (l&6)-kestotetraose. Fructose up to 50 mM did not affect 6-FEH activity; conversely, sucrose substantially inhibited the enzyme activity. Other disaccharides did not affect 6-FEH. It is suggested that sucrose might modulate 6-FEH activity in vivo.

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“…Barley fructan, like that from wheat and many other grasses, consists of a mixture of graminans, i.e. linear and branched fructans containing both b-(2,1) and b-(2,6) fructosyl linkages (Bancal et al 1991;Carpita et al 1991). According to the model for barley fructan biosynthesis (Duchateau et al 1995;Wiemken et al 1995), three enzymes, sucrose:sucrose 1-fructosyltransferase (1-SST), sucrose:fructan 6-fructosyltransferase (6-SFT) and fructan:fructan 1-fructosyltransferase (1-FFT), are necessary to synthesize all the fructan species in barley.…”

Section: Introductionmentioning

confidence: 99%

Fructan accumulation induced by nitrogen deficiency in barley leaves correlates with the level of sucrose:fructan 6-fructosyltransferase mRNA

Wang

Ende²,

Tillberg

2000

Planta

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Hydroponically cultivated barley plants were exposed to nitrogen (N)-deficiency followed by N-resupply. Metabolic and genetic regulation of fructan accumulation in the leaves were investigated. Fructan accumulated in barley leaves under N-deficiency was mobilized during N-resupply. The enhanced total activity of fructan-synthesizing enzymes, sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99) and sucrose:fructan 6-fructosyltransferase (6-SFT; EC 2.4. 1.10) caused by N-deficiency decreased with the mobilization of fructan during N-resupply. The activity of the barley fructan-degrading enzyme, fructan exohydrolyase (EC 3.2.1.80) was less affected by the N status. The low level of foliar soluble acid invertase activity under N-deficiency conditions was maintained during the commencement of N-resupply but increased subsequently. Further analyses by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, western blot and northern blot demonstrated that the fructan accumulation and the total activity of fructan-synthesizing enzymes correlated with the 6-SFT mRNA level. We suggest that the changes in fructan levels under N stress are intimately connected with the regulation of fructan synthetic rate which is mostly controlled by 6-SFT.

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New features of plant-fructan structure revealed by methylation analysis and carbon-13 n.m.r. spectroscopy

Cited by 59 publications

References 26 publications

Fructosyltransferase Activities in the Leaf Growth Zone of Tall Fescue

Fructosyltransferase Activities in the Leaf Growth Zone of Tall Fescue

Hydrolysis of fructan in grasses: a β‐(2‐6)‐linkage specific fructan‐β‐fructosidase from stubble of Lolium perenne

Fructan accumulation induced by nitrogen deficiency in barley leaves correlates with the level of sucrose:fructan 6-fructosyltransferase mRNA

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