Evidence map›Paper›PMID 30215129›Full record

ArticleApplied microbiology and biotechnology2018

Secretory expression of β-mannanase in Saccharomyces cerevisiae and its high efficiency for hydrolysis of mannans to mannooligosaccharides.

Junquan Liu, Abdul Basit, Ting Miao, Fengzhen Zheng, Hang Yu, Yan Wang, Wei Jiang, Yunhe Cao

Abstract read
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In one paragraph

Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

3 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Applications of Microbial β-Mannanases.Frontiers in bioengineering and biotechnology · 2020
    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

8 authors at 1 institution in 1 country.

Junquan LiuBeijing Advanced Innovation Center for Food Nutrition and Human Health, State Key Laboratory of Agro-Biotechnology, China Agricultural University, Beijing, China.
Abdul BasitBeijing Advanced Innovation Center for Food Nutrition and Human Health, State Key Laboratory of Agro-Biotechnology, China Agricultural University, Beijing, China.
Ting MiaoBeijing Advanced Innovation Center for Food Nutrition and Human Health, State Key Laboratory of Agro-Biotechnology, China Agricultural University, Beijing, China.
Fengzhen ZhengBeijing Advanced Innovation Center for Food Nutrition and Human Health, State Key Laboratory of Agro-Biotechnology, China Agricultural University, Beijing, China.
Hang YuLiaoning Union Pharmaceutical Company Limited, Benxi, Liaoning, China.
Yan WangLiaoning Union Pharmaceutical Company Limited, Benxi, Liaoning, China.
Wei JiangBeijing Advanced Innovation Center for Food Nutrition and Human Health, State Key Laboratory of Agro-Biotechnology, China Agricultural University, Beijing, China. jiangwei01@cau.edu.cn.ORCID http://orcid.org/0000-0002-1054-6360
Yunhe CaoState Key Laboratory of Animal Nutrition, China Agricultural University, Beijing, China. caoyh@cau.edu.cn.
China Agricultural University · CN

Funding

Scientific and Technical Supporting Programmes 2013BAD10B01
6 · The paper itself

Abstract

Degradation of mannans is a key process in the production of foods and prebiotics. β-Mannanase is the key enzyme that hydrolyzes 1,4-β-D-mannosidic linkages in mannans. Heterogeneous expression of β-mannanase in Pichia pastoris systems is widely used; however, Saccharomyces cerevisiae expression systems are more reliable and safer. We optimized β-mannanase gene from Aspergillus sulphureus and expressed it in five S. cerevisiae strains. Haploid and diploid strains, and strains with constitutive promoter TEF1 or inducible promoter GAL1, were tested for enzyme expression in synthetic auxotrophic or complex medium. Highest efficiency expression was observed for haploid strain BY4741 integrated with β-mannanase gene under constitutive promoter TEF1, cultured in complex medium. In fed-batch culture in a fermentor, enzyme activity reached ~ 24 U/mL after 36 h, and production efficiency reached 16 U/mL/day. Optimal enzyme pH was 2.0-7.0, and optimal temperature was 60 °C. In studies of β-mannanase kinetic parameters for two substrates, locust bean gum galactomannan (LBG) gave K

Indexed as

AspergillusBatch Cell Culture Techniquesbeta-MannosidaseDNA, FungalGalactansGalactokinaseGalactoseGene DosageGene Expression Regulation, EnzymologicHydrolysisIndustrial MicrobiologyMannansMannoseOligosaccharidesPichiaPlant Gums(1-6)-alpha-glucomannanbeta-MannosidaseDNA, FungalGAL1 protein, S cerevisiaeGalactansGalactokinasegalactomannanGalactoselocust bean gumMannansmannobiosemannopentaoseMannosemannotetraosemannotrioseOligosaccharidesPlant GumsSaccharomyces cerevisiae ProteinsTrisaccharidesExpressionMannansMannooligosaccharidesSaccharomyces cerevisiaeβ-Mannanase

Identifiers

PMID30215129
OpenAlexW2890058206

What OpenQuestion holds

Textmetadata
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.