Evidence map›Paper›PMID 35318423›Full record

ArticleCommunications biology2022

Metagenomic mining and structure-function studies of a hyper-thermostable cellobiohydrolase from hot spring sediment.

Migiwa Takeda, Seiki Baba, Jiro Okuma, Yoshitsugu Hirose, Asuka Nishimura, Masaki Takata, Kohei Oda, Daisuke Shibata, Takashi Kumasaka, Yasuhiro Kondo

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Lignocellulolytic extremozymes and their biotechnological applications.Extremophiles : life under extreme conditions · 2023
    Review
  5. Review
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

10 authors at 4 institutions in 1 country.

Migiwa TakedaHonda Research Institute Japan Co. Ltd., Kazusa Incubation Center, 2-1-5 Kazusa Kamatari, Kisarazu, Chiba, 292-0818, Japan.
Seiki BabaJapan Synchrotron Radiation Research Institute (JASRI), SPring-8, 1-1-1 Kouto, Sayo, Hyogo, 679-5148, Japan.
Jiro OkumaHonda Research Institute Japan Co. Ltd., Kazusa Incubation Center, 2-1-5 Kazusa Kamatari, Kisarazu, Chiba, 292-0818, Japan.
Yoshitsugu HiroseHonda Research Institute Japan Co. Ltd., Kazusa Incubation Center, 2-1-5 Kazusa Kamatari, Kisarazu, Chiba, 292-0818, Japan. yoshitsugu_hirose@jp.honda.ORCID 0000-0003-2320-8528
Asuka NishimuraHonda Research Institute Japan Co. Ltd., Kazusa Incubation Center, 2-1-5 Kazusa Kamatari, Kisarazu, Chiba, 292-0818, Japan.
Masaki TakataJapan Synchrotron Radiation Research Institute (JASRI), SPring-8, 1-1-1 Kouto, Sayo, Hyogo, 679-5148, Japan.
Kohei OdaHonda Research Institute Japan Co. Ltd., Kazusa Incubation Center, 2-1-5 Kazusa Kamatari, Kisarazu, Chiba, 292-0818, Japan.ORCID 0000-0003-3243-6629
Daisuke ShibataKazusa DNA Research Institute, 2-6-7 Kazusa-kamatari, Kisarazu, Chiba, 292-0812, Japan. shibata@kazusa.or.jp.ORCID 0000-0002-2384-595X
Takashi KumasakaJapan Synchrotron Radiation Research Institute (JASRI), SPring-8, 1-1-1 Kouto, Sayo, Hyogo, 679-5148, Japan. kumasaka@spring8.or.jp.ORCID 0000-0001-9289-1557
Yasuhiro KondoHonda Research Institute Japan Co. Ltd., Kazusa Incubation Center, 2-1-5 Kazusa Kamatari, Kisarazu, Chiba, 292-0818, Japan.
Honda (Japan) · JPSPring-8 · JPKazusa DNA Research Institute · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic breakdown is an attractive cellulose utilisation method with a low environmental load. Its high temperature operation could promote saccharification and lower contamination risk. Here we report a hyper-thermostable cellobiohydrolase (CBH), named HmCel6A and its variant HmCel6A-3SNP that were isolated metagenomically from hot spring sediments and expressed in Escherichia coli. They are classified into glycoside hydrolases family 6 (GH6). HmCel6A-3SNP had three amino acid replacements to HmCel6A (P88S/L230F/F414S) and the optimum temperature at 95 °C, while HmCel6A did it at 75 °C. Crystal structure showed conserved features among GH6, a (β/α)

Indexed as

Cellulose 1,4-beta-CellobiosidaseHot SpringsCelluloseCelluloseCellulose 1,4-beta-Cellobiosidase

Identifiers

PMID35318423
PMCPMC8940973
OpenAlexW4221060979

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.