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  • 1
    Electronic Resource
    Electronic Resource
    Arabidopsis AtcwINV3 and 6 are not invertases but are fructan exohydrolases (FEHs) with different substrate specificities (2005)
    Oxford, UK : Blackwell Science Ltd
    Plant, cell & environment 28 (2005), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The genome of Arabidopsis thaliana contains six putative cell-wall type invertase genes (AtcwINV1-6). Heterologous expression of AtcwINV1, 3 and 6 cDNAs in Pichia pastoris revealed that the enzymes encoded by AtcwINV3 and 6 did not show invertase activity. Instead, AtcwINV3 is a 6-FEH and AtcwINV6 is a fructan exohydrolase (FEH) that can degrade both inulin and levan-type fructans. For AtcwINV6 it is proposed to use the term (6&1) FEH. In contrast, AtcwINV1 is a typical invertase. FEH activity was also detected in crude extracts of different parts of Arabidopsis. To verify that the FEH activity of AtcwINV3 and 6 were not artefacts of the heterologous expression system, the protein corresponding to AtcwINV3 was isolated from whole Arabidopsis plants and indeed showed only 6-FEH activity and no invertase activity. Although no fructans can be detected in Arabidopsis plants, it is shown that kestoses (trimers) can be synthesized in crude leaf extracts. The putative physiological significance of FEH in so-called non-fructan plants is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3040.2004.01281.x
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular cloning and characterization of a high DP fructan: fructan 1-fructosyl transferase from Viguiera discolor (Asteraceae) and its heterologous expression in Pichia pastoris (2005)
    Oxford, UK; Malden, USA : Munksgaard International Publishers
    Physiologia plantarum 125 (2005), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Inulin-type fructans are stored in the tuberous roots of the Brazilian cerrado plant Viguiera discolor Baker (Asteraceae). In Cynara scolymus (artichoke) and Echinops ritro (globe thistle), the fructans have a considerably higher degree of polymerization (DP) than in Cichorium intybus (chicory) and Helianthus tuberosus (Jerusalem artichoke). It was shown before that the higher DP in some species can be attributed to the properties of their fructan: fructan 1-fructosyl transferases (1-FFTs; EC 2.4.1.100), enzymes responsible for chain elongation. Here, we describe the cloning of a high DP (hDP) 1-FFT cDNA from V. discolor and its heterologous expression in Pichia pastoris. Starting from 1-kestose and Neosugar P (a mixture of oligo-inulins from microbial origin) as substrates, the recombinant enzyme produces a typical hDP inulin profile in vitro, closely resembling the one observed in vivo. The enzyme shows no invertase activity and sucrose: sucrose 1-fructosyl transferase (1-SST; EC 2.4.1.99) activity in vitro. Pattern evolution during incubation suggests that inulins with DP ≥ 6 are much better substrates than sucrose or lower DP oligo-fructans. Because hDP inulin-type fructans show superior properties for specific food and non-food applications, the hDP 1-FFT gene from V. discolor has potential for the production of hDP inulin in vitro or in transgenic crops.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.2005.00579.x
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of strongly chitin-binding chitinases from salicylic acid-treated leek (Allium porrum) (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Six chitinases (EC 3.2.1.14) were purified from salicylate-treated leek (Allium porrum L.). They all strongly bind to chitin and can roughly be divided into two groups. One group has blocked N-termini, is completely inhibited by 1 mM AgNO3, has a relatively narrow pH optimum, a temperature optimum of 40°C and cannot degrade the tetramer of chitin. The other group has unblocked N-termini showing homology to the chitin-binding lectin WGA and is therefore considered as class I chitinases. This group is only moderately inhibited by 1 mM AgNO3 (30%), has a relatively broad pH optimum, has a higher temperature optimum (50 to 60°C) and can degrade the tetramer of chitin to dimers. Furthermore, all isoforms have molecular masses around 34 kDa as estimated by SDS-PAGE. They have isoelectric points ranging from 4 to 8 and no detectable lysozyme activity. Two isoforms investigated in more detail differ in their antifungal potential.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1040205.x
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