Evidence map›Paper›PMID 39342015›Full record

ArticleScientific reports2024

Combinatorial optimization of the hybrid cellulase complex structure designed from modular libraries.

Hikaru Nakazawa, Izumi Okada, Tomoyuki Ito, Yuri Ishigaki, Izumi Kumagai, Mitsuo Umetsu

Abstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

6 authors.

Hikaru NakazawaDepartment of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba 6-6-1, Aramaki, Aoba-Ku, Sendai, 980-8579, Japan. hikaru@tohoku.ac.jp.
Izumi OkadaDepartment of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba 6-6-1, Aramaki, Aoba-Ku, Sendai, 980-8579, Japan.
Tomoyuki ItoDepartment of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba 6-6-1, Aramaki, Aoba-Ku, Sendai, 980-8579, Japan.
Yuri IshigakiDepartment of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba 6-6-1, Aramaki, Aoba-Ku, Sendai, 980-8579, Japan.
Izumi KumagaiDepartment of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba 6-6-1, Aramaki, Aoba-Ku, Sendai, 980-8579, Japan.
Mitsuo UmetsuDepartment of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba 6-6-1, Aramaki, Aoba-Ku, Sendai, 980-8579, Japan. mitsuo@tohoku.ac.jp.

Funding

MEXT | Japan Science and Technology Agency (JST) Advanced Low Carbon Technology Research and Development Program GrantMEXT | Japan Society for the Promotion of Science (JSPS) 16H04570MEXT | Japan Society for the Promotion of Science (JSPS) 22K18911
6 · The paper itself

Abstract

Cellulase selectively recognizes cellulose surfaces and cleaves their β-1,4-glycosidic bonds. Combining hydrolysis using cellulase and fermentation can produce alternative fuels and chemical products. However, anaerobic bacteria produce only low levels of highly active cellulase complexes so-called cellulosomes. Therefore, we designed hybrid cellulase complexes from 49 biotinylated catalytic domain (CD) and 30 biotinylated cellulose-binding domain (CBD) libraries on streptavidin-conjugated nanoparticles to enhance cellulose hydrolysis by mimicking the cellulosome structure. The hybrid cellulase complex, incorporating both native CD and CBD, significantly improved reducing sugar production from cellulose compared to free native modular enzymes. The optimal CBD for each hybrid cellulase complex differed from that of the native enzyme. The most effective hybrid cellulase complex was observed with the combination of CD

Indexed as

CellulaseCelluloseBacterial ProteinsCatalytic DomainCellulosomesHydrolysisNanoparticlesBacterial ProteinsCellulaseCellulose

Identifiers

PMID39342015
PMCPMC11438973

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.