Evidence map›Paper›PMID 32245432›Full record

ArticleMicrobial cell factories2020

Improving cytosolic aspartate biosynthesis increases glucoamylase production in Aspergillus niger under oxygen limitation.

Weiqiang Cao, Guan Wang, Hongzhong Lu, Liming Ouyang, Ju Chu, Yufei Sui, Yingping Zhuang

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 21 citations in OpenAlex.

  1. Rewiring Amino Acid Flux for Efficient Transglutaminase Production inJournal of agricultural and food chemistry · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Impact of overexpressing NADH kinase on glucoamylase production in Aspergillus niger.Journal of industrial microbiology & biotechnology · 2022
    Article
  6. Article
  7. 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

7 authors at 1 institution in 1 country.

Weiqiang CaoState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China.
Guan WangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China.
Hongzhong LuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China.
Liming OuyangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China. ouyanglm@ecust.edu.cn.
Ju ChuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China.
Yufei SuiState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China.
Yingping ZhuangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China. ypzhuang@ecust.edu.cn.
East China University of Science and Technology · CN

Funding

Fundamental Research Funds for the Central Universities 22221818014Fundamental Research Funds for the Central Universities WF1814032National Key Research and Development Program of China 2019YFA0904800Science and Technology Commission of Shanghai Municipality 19ZR1413600
6 · The paper itself

Abstract

backgroundGlucoamylase is one of the most industrially applied enzymes, produced by Aspergillus species, like Aspergillus niger. Compared to the traditional ways of process optimization, the metabolic engineering strategies to improve glucoamylase production are relatively scarce.

resultsIn the previous study combined multi-omics integrative analysis and amino acid supplementation experiment, we predicted four amino acids (alanine, glutamate, glycine and aspartate) as the limited precursors for glucoamylase production in A. niger. To further verify this, five mutants namely OE-ala, OE-glu, OE-gly, OE-asp1 and OE-asp2, derived from the parental strain A. niger CBS 513.88, were constructed respectively for the overexpression of five genes responsible for the biosynthesis of the four kinds of amino acids (An11g02620, An04g00990, An05g00410, An04g06380 and An16g05570). Real-time quantitative PCR revealed that all these genes were successfully overexpressed at the mRNA level while the five mutants exhibited different performance in glucoamylase production in shake flask cultivation. Notably, the results demonstrated that mutant OE-asp2 which was constructed for reinforcing cytosolic aspartate synthetic pathway, exhibited significantly increased glucoamylase activity by 23.5% and 60.3% compared to CBS 513.88 in the cultivation of shake flask and the 5 L fermentor, respectively. Compared to A. niger CBS 513.88, mutant OE-asp2 has a higher intracellular amino acid pool, in particular, alanine, leucine, glycine and glutamine, while the pool of glutamate was decreased.

conclusionOur study combines the target prediction from multi-omics analysis with the experimental validation and proves the possibility of increasing glucoamylase production by enhancing limited amino acid biosynthesis. In short, this systematically conducted study will surely deepen the understanding of resources allocation in cell factory and provide new strategies for the rational design of enzyme production strains.

Indexed as

Aspartic AcidAspergillus nigerCytosolOxygenAspartic AcidOxygenAspergillus nigerGene overexpressionGlucoamylaseLimited amino acidsMulti-omics study

Identifiers

PMID32245432
PMCPMC7118866
OpenAlexW3014903401

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LicenceCC BY
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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.