Evidence map›Paper›PMID 29931209›Full record

ArticleJournal of experimental botany2018

Purification, characterization, and functional analysis of a novel 6G&1-FEH mainly hydrolyzing neokestose from asparagus.

Keiji Ueno, Takahiro Sonoda, Midori Yoshida, Norio Shiomi, Shuichi Onodera

Abstract read
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In one paragraph

Article in Journal of experimental botany, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

  1. A Fructan 6-Exohydrolase fromPlants (Basel, Switzerland) · 2026
    Article
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  6. Synbiotic microencapsulation ofJournal of food science and technology · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Keiji UenoDepartment of Food Sciences, Faculty of Dairy Science, Rakuno Gakuen University, Ebetsu, Japan.
Takahiro SonodaDepartment of Sustainable Agricultures, College of Agriculture, Food and Environment Sciences, Rakuno Gakuen University, Ebetsu, Japan.
Midori YoshidaNARO Hokkaido Agricultural Research Center, Hitsujigaoka, Sapporo, Japan.
Norio ShiomiDepartment of Food Sciences, Faculty of Dairy Science, Rakuno Gakuen University, Ebetsu, Japan.
Shuichi OnoderaDepartment of Food Science and Human Wellness, College of Agriculture, Food and Environment Sciences, Rakuno Gakuen University, Ebetsu, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Asparagus (Asparagus officinalis L.) accumulates inulin- and inulin neoseries-type fructans. Fructose released by the hydrolysis of fructans is an energy source for emerging asparagus spears. Plant fructans are hydrolyzed by fructan exohydrolases (FEHs), whose presence in asparagus has not yet been fully characterized. Here, we describe for the first time the purification and characterization of an FEH from asparagus, and the functional analysis of its gene. The purified enzyme was predicted to exist as a dimer (approximately 130 kDa) consisting of two polypeptides with a molecular mass of approximately 68 kDa. N-terminal sequences of the purified enzyme were matched with the amino acid sequences of aoeh4a and aoeh4b cDNAs isolated from asparagus (cv. Gijnlim and Taihouwase). Native enzymes obtained from asparagus roots and recombinant enzymes produced by Pichia pastoris showed fructan 1-exohydrolase (1-FEH) activity via the hydrolysis of inulin-type fructan. Unlike other 1-FEHs, these enzymes showed minimal hydrolysis of 1-kestose but efficiently hydrolyzed neokestose. Therefore, the enzyme was termed 6G&1-FEH. Gene expression studies in asparagus roots showed that aoeh4 increased during root storage at 2 °C and spear harvesting. These findings suggest that 6G&1-FEH may be involved in fructan hydrolysis in asparagus roots to provide an energy source for emerging asparagus spears.

Indexed as

Amino Acid SequenceAsparagus PlantGlycoside HydrolasesHydrolysisPhylogenyPlant ProteinsSequence AlignmentTrisaccharidesGlycoside HydrolasesneokestosePlant ProteinsTrisaccharides

Identifiers

PMID29931209

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.