A fructan exohydrolase from maize degrades both inulin and levan and co-exists with 1-kestotriose in maize
Enzymes with fructan exohydrolase (FEH) activity are present not only in fructan-synthesizing species but also in non-fructan plants. This has led to speculation about their functions in non-fructan species. Here, a cell wall invertase-related Zm-6&1-FEH2 with no “classical” invertase motif was...
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| Main Authors: | , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
13 May 2021
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| In: |
International journal of molecular sciences
Year: 2021, Volume: 22, Issue: 10, Pages: 1-14 |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms22105149 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.3390/ijms22105149 Verlag, lizenzpflichtig, Volltext: https://www.mdpi.com/1422-0067/22/10/5149 |
| Author Notes: | Silin Wu, Steffen Greiner, Chongjian Ma, Jiaxin Zhong, Xiaojia Huang, Thomas Rausch and Hongbo Zhao |
| Summary: | Enzymes with fructan exohydrolase (FEH) activity are present not only in fructan-synthesizing species but also in non-fructan plants. This has led to speculation about their functions in non-fructan species. Here, a cell wall invertase-related Zm-6&1-FEH2 with no “classical” invertase motif was identified in maize. Following heterologous expression in Pichia pastoris and in Nicotiana benthamiana leaves, the enzyme activity of recombinant Zm-6&1-FEH2 displays substrate specificity with respect to inulin and levan. Subcellular localization showed Zm-6&1-FEH2 exclusively localized in the apoplast, and its expression profile was strongly dependent on plant development and in response to drought and abscisic acid. Furthermore, formation of 1-kestotriose, an oligofructan, was detected in vivo and in vitro and could be hydrolyzed by Zm-6&1-FEH2. In summary, these results support that Zm-6&1-FEH2 enzyme from maize can degrade both inulin-type and levan-type fructans, and the implications of the co-existence of Zm-6&1-FEH2 and 1-kestotriose are discussed. |
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| Item Description: | Gesehen am 06.09.2021 |
| Physical Description: | Online Resource |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms22105149 |