Evidence map›Paper›PMID 33394289›Full record

ArticleApplied biochemistry and biotechnology2021

Substrate Specificities of GH8, GH39, and GH52 β-xylosidases from Bacillus halodurans C-125 Toward Substituted Xylooligosaccharides.

Koji Teramoto, Sosyu Tsutsui, Tomoko Sato, Zui Fujimoto, Satoshi Kaneko

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Article in Applied biochemistry and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Feasibility insights into the application ofFrontiers in microbiology · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Koji TeramotoDepartment of Subtropical Biochemistry and Biotechnology, Faculty of Agriculture, University of the Ryukyus, 1 Senbaru, Nishihara, Okinawa, 903-0213, Japan.
Sosyu TsutsuiDepartment of Subtropical Biochemistry and Biotechnology, Faculty of Agriculture, University of the Ryukyus, 1 Senbaru, Nishihara, Okinawa, 903-0213, Japan.
Tomoko SatoAdvanced Analysis Center, National Agriculture and Food Research Organization (NARO), 2-1-2 Kannondai, Tsukuba, 305-8602, Japan.
Zui FujimotoAdvanced Analysis Center, National Agriculture and Food Research Organization (NARO), 2-1-2 Kannondai, Tsukuba, 305-8602, Japan.
Satoshi KanekoDepartment of Subtropical Biochemistry and Biotechnology, Faculty of Agriculture, University of the Ryukyus, 1 Senbaru, Nishihara, Okinawa, 903-0213, Japan. sakaneko@agr.u-ryukyu.ac.jp.ORCID https://orcid.org/0000-0001-9169-9731

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Substrate specificities of glycoside hydrolase families 8 (Rex), 39 (BhXyl39), and 52 (BhXyl52) β-xylosidases from Bacillus halodurans C-125 were investigated. BhXyl39 hydrolyzed xylotriose most efficiently among the linear xylooligosaccharides. The activity decreased in the order of xylohexaose > xylopentaose > xylotetraose and it had little effect on xylobiose. In contrast, BhXyl52 hydrolyzed xylobiose and xylotriose most efficiently, and its activity decreased when the main chain became longer as follows: xylotetraose > xylopentaose > xylohexaose. Rex produced O-β-D-xylopyranosyl-(1 → 4)-[O-α-L-arabinofuranosyl-(1 → 3)]-O-β-D-xylopyranosyl-(1 → 4)-β-D-xylopyranose (Ara

Indexed as

BacillusBacterial ProteinsGlucuronatesHydrolysisOligosaccharidesSubstrate SpecificityXylosidasesBacterial Proteinsexo-1,4-beta-D-xylosidaseGlucuronatesOligosaccharidesxylooligosaccharideXylosidasesAldouronic acidArabinoxylooligosaccharideGlucronoxylooligosaccharideGlycoside hydrolase family 39Glycoside hydrolase family 52Glycoside hydrolase family 8β-D-xylosidase

Identifiers

PMID33394289

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.