Journal of Applied Glycoscience
Online ISSN : 1880-7291
Print ISSN : 1344-7882
ISSN-L : 1344-7882
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Two Fructan 1-Exohydrolase Isoforms Hydrolyze Fructans in Edible Burdock (Arctium lappa L.) during Storage at a Low Temperature
Keiji UenoSatoru YokoshimaYuki SasajimaYojiro IshiguroMidori YoshidaNorio ShiomiShuichi Onodera
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2015 Volume 62 Issue 2 Pages 65-72

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Abstract

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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© 2015 by The Japanese Society of Applied Glycoscience
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