Evidence map›Paper›PMID 27555836›Full record

ArticleFrontiers in microbiology2016

Production of Thermostable Organic Solvent Tolerant Keratinolytic Protease from Thermoactinomyces sp. RM4: IAA Production and Plant Growth Promotion.

Amit Verma, Hukum Singh, Mohammad S Anwar, Shailendra Kumar, Mohammad W Ansari, Sanjeev Agrawal

Abstract read
In one paragraph

Article in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Keratinolytic proteases secreted by Bacillus subtilis obtained from feather-based submerged culture.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
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  8. Article
  9. Article
  10. Article
  11. Review
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  13. Article
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  15. Article
  16. Citrobacter diversus-derived keratinases and their potential application as detergent-compatible cloth-cleaning agents.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020
    Article
  17. Article
  18. Review
  19. 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

6 authors.

Amit VermaDepartment of Biochemistry, G. B. Pant University of Agriculture and TechnologyPantnagar, India; College of Basic Science & Humanities, Sardarkrushinagar Dantiwada Agricultural UniversityPalanpur, India.
Hukum SinghClimate Change and Forest Influence Division, Forest Research Institute Dehradun, India.
Mohammad S AnwarDepartment of Biotechnology, Bheemtal Campus, Kumaun University Nainital, India.
Shailendra KumarForest Pathology Division, Forest Research Institute Dehradun, India.
Mohammad W AnsariDepartment of Botany, Zakir Husain Delhi College, University of Delhi New Delhi, India.
Sanjeev AgrawalDepartment of Biochemistry, G. B. Pant University of Agriculture and Technology Pantnagar, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There are several reports about the optimization of protease production, but only few have optimized the production of organic solvent tolerant keratinolytic proteases that show remarkable exploitation in the development of the non-polluting processes in biotechnological industries. The present study was carried with aim to optimize the production of a thermostable organic solvent tolerant keratinolytic protease Thermoactinomyces sp. RM4 utilizing chicken feathers. Thermoactinomyces sp. RM4 isolated from the soil sample collected from a rice mill wasteyard site near Kashipur, Uttrakhand was identified on the basis of 16S rDNA analysis. The production of organic solvent tolerant keratinolytic protease enzyme by Thermoactinomyces sp. RM4 was optimized by varying physical culture conditions such as pH (10.0), temperature (60°C), inoculum percentage (2%), feather concentration (2%) and agitation rate (2 g) for feather degradation. The result showed that Thermoactinomyces sp. RM4 potentially produces extra-cellular thermostable organic solvent tolerant keratinolytic protease in the culture medium. Further, the feather hydrolysate from keratinase production media showed plant growth promoting activity by producing indole-3-acetic acid itself. The present findings suggest that keratinolytic protease from Thermoactinomyces sp. RM4 offers enormous industrial applications due to its organic solvent tolerant property in peptide synthesis, practical role in feather degradation and potential function in plant growth promoting activity, which might be a superior candidate to keep ecosystem healthy and functional.

Indexed as

ecosystem healthfeather degradationindole-3-acetic acid productionkeratinaseorganic solvent stabilityThermoactinomyces

Identifiers

PMID27555836
PMCPMC4974946

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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.