Evidence map›Paper›PMID 22480329›Full record

ArticleAquatic biosystems2012

Function and biotechnology of extremophilic enzymes in low water activity.

Ram Karan, Melinda D Capes, Shiladitya Dassarma

Open access · hybridAbstract read
In one paragraph

Article in Aquatic biosystems, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed, 1 pooled it
14.5field-weighted citation impact, top 1% 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

80 citing papers in PubMed, 1 synthesis or guideline pooled it, 251 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. A third type of PETase from the marine Halopseudomonas lineage.Protein science : a publication of the Protein Society · 2025
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  10. Article
  11. Review
  12. Article
  13. Article
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  15. Review
  16. Article
  17. Comparative Genomics ofMicroorganisms · 2023
    Article
  18. Article
  19. A novel salt- and organic solvent-tolerant phosphite dehydrogenase fromFrontiers in bioengineering and biotechnology · 2023
    Article
  20. Characterization ofMicrobiology spectrum · 2022
    Article

20 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Ram KaranDepartment of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD, USA. sdassarma@som.umaryland.edu.
Melinda D Capes
Shiladitya Dassarma
University System of Maryland · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes from extremophilic microorganisms usually catalyze chemical reactions in non-standard conditions. Such conditions promote aggregation, precipitation, and denaturation, reducing the activity of most non-extremophilic enzymes, frequently due to the absence of sufficient hydration. Some extremophilic enzymes maintain a tight hydration shell and remain active in solution even when liquid water is limiting, e.g. in the presence of high ionic concentrations, or at cold temperature when water is close to the freezing point. Extremophilic enzymes are able to compete for hydration via alterations especially to their surface through greater surface charges and increased molecular motion. These properties have enabled some extremophilic enzymes to function in the presence of non-aqueous organic solvents, with potential for design of useful catalysts. In this review, we summarize the current state of knowledge of extremophilic enzymes functioning in high salinity and cold temperatures, focusing on their strategy for function at low water activity. We discuss how the understanding of extremophilic enzyme function is leading to the design of a new generation of enzyme catalysts and their applications to biotechnology.

Identifiers

PMID22480329
PMCPMC3310334
OpenAlexW2135989046

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.