Evidence map›Paper›PMID 27016935›Full record

ArticleJournal of industrial microbiology & biotechnology2016

Heterologous expression and characterization of a new heme-catalase in Bacillus subtilis 168.

Tuyishime Philibert, Zhiming Rao, Taowei Yang, Junping Zhou, Genshu Huang, Komera Irene, Niyomukiza Samuel

Abstract read
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In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Degradation Mechanism of Aflatoxin MFoods (Basel, Switzerland) · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Engineering Bacillus subtilis ATCC 6051a for the production of recombinant catalases.Journal of industrial microbiology & biotechnology · 2021
    Article
  7. Article
  8. A novel expression vector for the secretion of abaecin in Bacillus subtilis.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]
    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.

Tuyishime PhilibertThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, 214122, Wuxi, Jiangsu, People's Republic of China.
Zhiming RaoThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, 214122, Wuxi, Jiangsu, People's Republic of China. raozhm@jiangnan.edu.cn.
Taowei YangThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, 214122, Wuxi, Jiangsu, People's Republic of China.
Junping ZhouThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, 214122, Wuxi, Jiangsu, People's Republic of China.
Genshu HuangThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, 214122, Wuxi, Jiangsu, People's Republic of China.
Komera IreneThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, 214122, Wuxi, Jiangsu, People's Republic of China.
Niyomukiza SamuelThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, 214122, Wuxi, Jiangsu, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reactive oxygen species (ROS) is an inherent consequence to all aerobically living organisms that might lead to the cells being lethal and susceptible to oxidative stress. Bacillus pumilus is characterized by high-resistance oxidative stress that stimulated our interest to investigate the heterologous expression and characterization of heme-catalase as potential biocatalyst. Results indicated that recombinant enzyme significantly exhibited the high catalytic activity of 55,784 U/mg expressed in Bacillus subtilis 168 and 98.097 µmol/min/mg peroxidatic activity, the apparent K m of catalytic activity was 59.6 ± 13 mM with higher turnover rate (K cat = 322.651 × 10(3) s(-1)). The pH dependence of catalatic and peroxidatic activity was pH 7.0 and pH 4.5 respectively with temperature dependence of 40 °C and the recombinant heme-catalase exhibited a strong Fe(2+) preference. It was further revealed that catalase KatX2 improved the resistance oxidative stress of B. subtilis. These findings suggest that this B. pumilus heme-catalase can be considered among the industrially relevant biocatalysts due to its exceptional catalytic rate and high stability and it can be a potential candidate for the improvement of oxidative resistance of industrially produced strains.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SequenceBacillus subtilisBacterial ProteinsCatalaseCloning, MolecularHydrogen-Ion ConcentrationIndustrial MicrobiologyModels, MolecularOxidative StressPhylogenyProtein ConformationRecombinant ProteinsRNA, Ribosomal, 16SSequence Analysis, DNABacterial ProteinsCatalaseRecombinant ProteinsRNA, Ribosomal, 16SBacillus pumilusCharacteristicHeme-catalaseOxidative stress

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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.