Evidence map›Paper›PMID 39971319›Full record

ArticleProceedings of the Japan Academy. Series B, Physical and biological sciences2025

A thermostable and highly active fungal GH3 β-glucosidase generated by random and saturation mutagenesis.

Chiaki Matsuzaki, Masafumi Hidaka, Yukari Nakashima, Yuji Honda, Takashi Koyanagi, Kazuhiko Ishikawa, Toshihiko Katoh, Takane Katayama, Hidehiko Kumagai

Abstract read
In one paragraph

Article in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

9 authors.

Chiaki MatsuzakiResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.ORCID http://orcid.org/0000-0001-6035-0481
Masafumi HidakaGraduate School of Agricultural Science, Division of Agricultural Chemistry, Tohoku University, Sendai, Miyagi, Japan.ORCID http://orcid.org/0000-0003-3458-1707
Yukari NakashimaResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.
Yuji HondaDepartment of Food Science, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.
Takashi KoyanagiDepartment of Food Science, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.ORCID http://orcid.org/0000-0003-3688-0022
Kazuhiko IshikawaRare Sugar and Enzyme Research, Dep. I, R&D, Matsutani Chemical Industry Co. Ltd., Itami, Hyogo, Japan.ORCID http://orcid.org/0000-0001-9845-0461
Toshihiko KatohResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.ORCID http://orcid.org/0000-0002-7996-5619
Takane KatayamaResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.ORCID http://orcid.org/0000-0003-4009-7874
Hidehiko KumagaiResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.ORCID http://orcid.org/0000-0003-2464-3249

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enhancing the thermostability of cellulose-degrading enzymes is pivotal for establishing an efficient bioconversion system from cellulosic materials to value-added compounds. Here, by introducing random and saturation mutagenesis into the Thermoascus aurantiacus β-glucosidase gene, we generated a hyperthermostable mutant with five amino acid substitutions. Analysis of temperature-induced unfolding revealed the involvement of each replacement in the increased T

Indexed as

beta-GlucosidaseMutagenesisThermoascusAmino Acid SubstitutionCellobioseCrystallographyEnzyme StabilityEscherichia coliKluyveromycesRecombinant Proteinsbeta-GlucosidaseCellobioseRecombinant Proteinscellulasecrystal structureKluyveromyces marxianusThermoascus aurantiacusthermostableβ-glucosidase

Identifiers

PMID39971319
PMCPMC12321500

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

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.