Evidence map›Paper›PMID 27594915›Full record

ArticleBiotechnology for biofuels2016

From mannan to bioethanol: cell surface co-display of β-mannanase and β-mannosidase on yeast Saccharomyces cerevisiae.

Jun Ishii, Fumiyoshi Okazaki, Apridah Cameliawati Djohan, Kiyotaka Y Hara, Nanami Asai-Nakashima, Hiroshi Teramura, Ade Andriani, Masahiro Tominaga, Satoshi Wakai, Prihardi Kahar and 4 more

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Research and application progress of microbial β-mannanases: a mini-review.World journal of microbiology & biotechnology · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Cell-surface engineering of yeasts for whole-cell biocatalysts.Bioprocess and biosystems engineering · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

14 authors at 2 institutions in 2 countries.

Jun Ishii *Graduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Fumiyoshi Okazaki *Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Apridah Cameliawati DjohanResearch Center for Biotechnology, Indonesian Institute of Sciences (LIPI), Cibinong Jalan Raya Bogor Km. 46, Cibinong, West Java 16911 Indonesia.
Kiyotaka Y HaraOrganization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Nanami Asai-NakashimaGraduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Hiroshi TeramuraGraduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Ade AndrianiResearch Center for Biotechnology, Indonesian Institute of Sciences (LIPI), Cibinong Jalan Raya Bogor Km. 46, Cibinong, West Java 16911 Indonesia.
Masahiro TominagaGraduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Satoshi WakaiGraduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Prihardi KaharDepartment of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
YopiResearch Center for Biotechnology, Indonesian Institute of Sciences (LIPI), Cibinong Jalan Raya Bogor Km. 46, Cibinong, West Java 16911 Indonesia.
Bambang PrasetyaResearch Center for Biotechnology, Indonesian Institute of Sciences (LIPI), Cibinong Jalan Raya Bogor Km. 46, Cibinong, West Java 16911 Indonesia.
Chiaki OginoDepartment of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Akihiko KondoGraduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501 Japan.
Kobe University · JPIndonesian Institute of Sciences · ID

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMannans represent the largest hemicellulosic fraction in softwoods and also serve as carbohydrate stores in various plants. However, the utilization of mannans as sustainable resources has been less advanced in sustainable biofuel development. Based on a yeast cell surface-display technology that enables the immobilization of multiple enzymes on the yeast cell walls, we constructed a recombinant Saccharomyces cerevisiae strain that co-displays β-mannanase and β-mannosidase; this strain is expected to facilitate ethanol fermentation using mannan as a biomass source.

resultsParental yeast S. cerevisiae assimilated mannose and glucose as monomeric sugars, producing ethanol from mannose. We constructed yeast strains that express tethered β-mannanase and β-mannosidase; co-display of the two enzymes on the cell surface was confirmed by immunofluorescence staining and enzyme activity assays. The constructed yeast cells successfully hydrolyzed 1,4-β-d-mannan and produced ethanol by assimilating the resulting mannose without external addition of enzymes. Furthermore, the constructed strain produced ethanol from 1,4-β-d-mannan continually during the third batch of repeated fermentation. Additionally, the constructed strain produced ethanol from ivory nut mannan; ethanol yield was improved by NaOH pretreatment of the substrate.

conclusionsWe successfully displayed β-mannanase and β-mannosidase on the yeast cell surface. Our results clearly demonstrate the utility of the strain co-displaying β-mannanase and β-mannosidase for ethanol fermentation from mannan biomass. Thus, co-tethering β-mannanase and β-mannosidase on the yeast cell surface provides a powerful platform technology for yeast fermentation toward the production of bioethanol and other biochemicals from lignocellulosic materials containing mannan components.

Indexed as

BiofuelBiomass resourceCell surface displayEthanolFermentationMannanMannanaseMannosidaseSaccharomyces cerevisiaeYeast

Identifiers

PMID27594915
PMCPMC5009545
OpenAlexW2513962985

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.