Two fructan 1-exohydrolase isoforms hydrolyze fructans in edible burdock (Arctium lappa L.) during storage at a low temperature
2015
Ueno, K. (Rakuno Gakuen University, Ebetsu, Hokkaido (Japan). Graduate School of Dairy Science Research, Department of Food and Nutrition Sciences) | Yokoshima, S. | Sasajima, Y. | Ishiguro, Y. | Yoshida, M. | Shiomi, N. | Onodera, S.
Edible burdock (Arctium lappa L.) accumulates an inulin-type fructan. Inulin-type fructan in plant has been hydrolyzed by fructan 1-exohydrolases (1-FEH). We have previously reported on the cloning of aleh1, which encodes a 1-FEH in edible burdock. Here, we describe the cloning of aleh2, which encodes a 1-FEH isozyme in edible burdock, and the functional analysis of the recombinant protein of aleh2 (rAlEH2) that displays properties different from the aleh1 recombinant protein. A cDNA, named aleh2, was obtained by the RACE. The rAlEH2, which was produced by Pichia pastoris, showed 1-FEH activity. Unlike the recombinant protein of aleh1, the rAlEH2 is a 1-FEH enzyme that efficiently hydrolyzes longer-chain fructans than 1-kestose, such as nystose, fructosylnystose and inulin. The expression study in burdock revealed the induction of aleh1 and aleh2 genes by low temperature. These findings indicated that two 1-FEH isoforms were involved in the degradation of the fructan in burdock roots during low-temperature storage.
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