Evidence map›Paper›PMID 32015452›Full record

ArticleScientific reports2020

Immobilization of β-Glucosidase from Thermatoga maritima on Chitin-functionalized Magnetic Nanoparticle via a Novel Thermostable Chitin-binding Domain.

Fawze Alnadari, Yemin Xue, Liang Zhou, Yahya S Hamed, Mohamed Taha, Mohamed F Foda

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  7. Biocatalytic Performance ofMicromachines · 2024
    Article
  8. Article
  9. Microbial β-glucanases: production, properties, and engineering.World journal of microbiology & biotechnology · 2023
    Review
  10. Article
  11. Article
  12. Evaluation of MScientific reports · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. Thiolation of Myco-Synthesized FeJournal of fungi (Basel, Switzerland) · 2022
    Article
  17. The Stability Improvement ofBiochemistry research international · 2022
    Article
  18. Article
  19. Review
  20. 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

6 authors at 5 institutions in 4 countries.

Fawze Alnadari *Department of Food Science and Engineering, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210023, Jiangsu, P.R. China.
Yemin Xue *Department of Food Science and Engineering, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210023, Jiangsu, P.R. China.
Liang ZhouDepartment of Food Science and Engineering, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210023, Jiangsu, P.R. China.
Yahya S HamedFood Technology Department, Faculty of Agriculture, Suez Canal University, Ismailia, 41522, Egypt.
Mohamed TahaDepartment of Biochemistry, Faculty of Agriculture, Benha University, Moshtohor, Toukh, 13736, Egypt.
Mohamed F FodaState Key Laboratory of Agricultural Microbiology, College of Science, Huazhong Agricultural University, Wuhan, 430070, P. R. China. m.frahat@fagr.bu.edu.eg.
Nanjing Normal University · CNHuazhong Agricultural University · CNRMIT University · AUSana'a University · YESuez Canal University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme immobilization is a powerful tool not only as a protective agent against harsh reaction conditions but also for the enhancement of enzyme activity, stability, reusability, and for the improvement of enzyme properties as well. Herein, immobilization of β-glucosidase from Thermotoga maritima (Tm-β-Glu) on magnetic nanoparticles (MNPs) functionalized with chitin (Ch) was investigated. This technology showed a novel thermostable chitin-binding domain (Tt-ChBD), which is more desirable in a wide range of large-scale applications. This exclusive approach was fabricated to improve the Galacto-oligosaccharide (GOS) production from a cheap and abundant by-product such as lactose through a novel green synthesis route. Additionally, SDS-PAGE, enzyme activity kinetics, transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FT-IR) revealed that among the immobilization strategies for Thermotoga maritime-β-Glucosidase thermostable chitin-binding domain (Tm-β-Glu-Tt-ChBD) on the attractive substrate; Ch-MNPs had the highest enzyme binding capacity and GOS production ratio when compared to the native enzyme. More interestingly, a magnetic separation technique was successfully employed in recycling the immobilized Tm-β-Glu for repetitive batch-wise GOS without significant loss or reduction of enzyme activity. This immobilization system displayed an operative stability status under various parameters, for instance, temperature, pH, thermal conditions, storage stabilities, and enzyme kinetics when compared with the native enzyme. Conclusively, the GOS yield and residual activity of the immobilized enzyme after the 10

Indexed as

Bacterial Proteinsbeta-GlucosidaseChitinEnzymes, ImmobilizedEnzyme StabilityKineticsMagnetite NanoparticlesModels, MolecularOligosaccharidesProtein DomainsRecombinant Fusion ProteinsTemperatureThermotoga maritimaBacterial Proteinsbeta-GlucosidaseChitinEnzymes, ImmobilizedMagnetite NanoparticlesOligosaccharidesRecombinant Fusion Proteins

Identifiers

PMID32015452
PMCPMC6997207
OpenAlexW3003736535

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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.