Evidence map›Paper›PMID 32524454›Full record

ArticleJournal of industrial microbiology & biotechnology2020

Enhanced production of β-alanine through co-expressing two different subtypes of L-aspartate-α-decarboxylase.

Lei Wang, Xiaoyu Piao, Shumei Cui, Meirong Hu, Yong Tao

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.0field-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

12 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  5. Article
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  7. Article
  8. Advances in the synthesis of β-alanine.Frontiers in bioengineering and biotechnology · 2023
    Review
  9. Study on the construction technology of β-alanine synthesizingFrontiers in bioengineering and biotechnology · 2023
    Article
  10. Article
  11. Article
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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

5 authors at 2 institutions in 1 country.

Lei WangChinese Academy of Sciences Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.ORCID http://orcid.org/0000-0003-2887-6322
Xiaoyu PiaoChinese Academy of Sciences Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Shumei CuiChinese Academy of Sciences Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Meirong HuChinese Academy of Sciences Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Yong TaoChinese Academy of Sciences Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. taoyong@im.ac.cn.
Institute of Microbiology · CNChinese Academy of Sciences · CN

Funding

National Key R&D Program of China 2017YFD0502102-3
6 · The paper itself

Abstract

β-Alanine (β-Ala) is an important intermediate with numerous applications in food and feed additives, pharmaceuticals, polymeric materials, and electroplating industries. Its biological production routes that employ L-aspartate-α-decarboxylase (ADC) as the key enzyme are attractive. In this study, we developed an efficient and environmentally safe method for β-Ala production by co-expressing two different subtypes of ADC. A bacterial ADC from Bacillus subtilis (BSADC) and an insect ADC from Tribolium castaneum (TCADC) use pyruvoyl and pyridoxal-5'-phosphate (PLP) as cofactor, respectively. 3050 mM (271.5 g/L) β-Ala was achieved from L-aspartic acid by using the whole-cell biocatalyst co-expressing BSADC and TCADC, corresponding to a conversion rate of 92.4%. Meanwhile, one-pot synthesis of β-Ala from fumaric acid through using a tri-enzyme cascade route with two different subtypes of ADC and L-aspartase (AspA) from Escherichia coli was established. 2250 mM (200.3 g/L) β-Ala was obtained from fumaric acid with a conversion rate of 90.0%. This work proposes a novel strategy that improves β-Ala production in the decarboxylation pathway of L-aspartic acid.

Indexed as

AnimalsAspartate Ammonia-LyaseAspartic AcidBacillus subtilisbeta-AlanineBiotechnologyBiotransformationCarboxy-LyasesCatalysisCulture MediaEscherichia coliFumaratesGlutamate DecarboxylaseHydrogen-Ion ConcentrationTemperatureTriboliumaspartate 4-decarboxylaseaspartate-alpha-decarboxylaseAspartate Ammonia-LyaseAspartic Acidbeta-AlanineCarboxy-LyasesCulture MediaFumaratesfumaric acidGlutamate DecarboxylaseCo-expressionL-aspartaseL-aspartate-α-decarboxylaseTri-enzyme cascadeWhole-cell biocatalystβ-alanine

Identifiers

PMID32524454
OpenAlexW3033808743

What OpenQuestion holds

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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.