Inulin synthesis by a combination of purified fructosyltransferases from tubers of Helianthus tuberosus
| Autor: | Norbert Sprenger, Andres Wiemken, Urs Hochstrasser, Marcel Lüscher, Thomas Boller, Christian Erdin |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
0106 biological sciences
Sucrose Glycoside Hydrolases Inulin Molecular Sequence Data Biophysics Oligosaccharides 01 natural sciences Biochemistry Fructan 03 medical and health sciences chemistry.chemical_compound Fructan-fructan 1-fructosyltransferase Tetramer Structural Biology Genetics Amino Acid Sequence Helianthus Molecular Biology Peptide sequence 030304 developmental biology chemistry.chemical_classification Sucrose-sucrose 1-fructosyltransferase 0303 health sciences biology beta-Fructofuranosidase Isoelectric focusing Helianthus tuberosus Cell Biology biology.organism_classification Peptide Fragments Amino acid Isoenzymes Molecular Weight Enzyme chemistry Hexosyltransferases Trisaccharides 010606 plant biology & botany |
| Zdroj: | FEBS letters. 385(1-2) |
| ISSN: | 0014-5793 |
| Popis: | Sucrose-sucrose 1-fructosyltransferase (1-SST) was purified 100-fold from tubers of Helianthus tuberosus L. The purified enzyme was essentially devoid of invertase activity and could be separated by isoelectric focusing into five isoforms which all were composed of two subunits (59 and 26 kDa). Fructan-fructan 1-fructosyltransferase (1-FFT) was purified from the same source [M. Lüscher et al. (1993) New Phytologist 123, 437–442). When incubated individually with sucrose, 1-FFT was inactive while 1-SST formed isokestose (trimer) and, upon prolonged incubation, some nystose (tetramer). When a combination of the two enzymes was incubated with sucrose, a series of oligofructosides with a degree of polymerization of up to 20 was formed. Amino acid sequences of tryptic peptide fragments from both 1-SST and 1-FFT indicate that these enzymes are highly homologous with plant invertases. |
| Databáze: | OpenAIRE |
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