Evidence map›Paper›PMID 32725297›Full record

ReviewJournal, genetic engineering & biotechnology2020

Adaptation, production, and biotechnological potential of cold-adapted proteases from psychrophiles and psychrotrophs: recent overview.

Junaid Furhan

Abstract readReview
In one paragraph

Review in Journal, genetic engineering & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Research Progress Regarding PsychrotrophicFoods (Basel, Switzerland) · 2025
    Review
  5. Article
  6. Review
  7. Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst.International journal of molecular sciences · 2023
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Cold Denaturation of Proteins in the Absence of Solvent: Implications for Protein Storage.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. Review
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  19. 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

1 author.

Junaid FurhanDepartment of Microbiology, SKIMS Medical College-Hospital, Bemina, Srinagar, Jammu and Kashmir, 190017, India. junaidfurhan86@gmail.com.ORCID https://orcid.org/0000-0002-4067-5753

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProteases or peptidases are an imperative class of hydrolytic enzymes capable of hydrolyzing large proteins into smaller peptides. The cold-adapted proteases show higher catalytic capacity in low temperatures as well as stability in alkaline conditions and appear as strong contenders for various applications in special industries. MAIN BODY: In the past few decades, the interest in cold-adapted microorganisms producing cold-adapted proteases has increased at an exciting rate, and many of them have emerged as important biotechnological and industrial candidates. Industrial proteases are largely supplied from various types of microorganisms than plant or animal sources. Among diverse microbial sources, psychrophiles and psychrotrophs inhabiting permanently or partially cold environments have appeared as rich sources of cold-adapted proteases. SHORT

conclusionThe present review focuses on recent sources of cold-adapted protease producers along with the molecular adaptation of psychrotrophs and psychrophiles. The recent knowledge on production, kinetic properties, purification, and substrate specificity of cold-adapted proteases has been summarized. Recent advances in cold-adapted protease gene cloning and structural studies are also described. Moreover, the prospective applications of cold-adapted proteases are discussed which can help in evaluating their industrial potential.

Indexed as

and PsychrotrophsCold-adapted proteasesEnzymesPsychrophiles

Identifiers

PMID32725297
PMCPMC7387391

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