Evidence map›Paper›PMID 24895537›Full record

ReviewBiochemistry research international2014

Microbial tyrosinases: promising enzymes for pharmaceutical, food bioprocessing, and environmental industry.

Kamal Uddin Zaidi, Ayesha S Ali, Sharique A Ali, Ishrat Naaz

Open access · goldAbstract readReview
In one paragraph

Review in Biochemistry research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

47 citing papers in PubMed, 169 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Sources and Applications of Tyrosinase in Life Sciences.Current pharmaceutical biotechnology · 2025
    Review
  9. Review
  10. Biochemical andMedicinal chemistry (Shariqah (United Arab Emirates)) · 2024
    Article
  11. Potent inhibition of human tyrosinase inhibitor by verproside from the whole plant ofJournal of enzyme inhibition and medicinal chemistry · 2023
    Article
  12. Article
  13. Tyrosinase Inhibitors: A Perspective.Molecules (Basel, Switzerland) · 2023
    Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

Kamal Uddin ZaidiMolecular Biotechnology Laboratory, Centre for Scientific Research & Development, People's University, Bhanpur, Bhopal 462010, India ; Department of Biotechnology, Saifia College of Science, Bhopal 462001, India.
Ayesha S AliDepartment of Biotechnology, Saifia College of Science, Bhopal 462001, India.
Sharique A AliDepartment of Biotechnology, Saifia College of Science, Bhopal 462001, India.
Ishrat NaazDepartment of Biotechnology, Saifia College of Science, Bhopal 462001, India.
People’s University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosinase is a natural enzyme and is often purified to only a low degree and it is involved in a variety of functions which mainly catalyse the o-hydroxylation of monophenols into their corresponding o-diphenols and the oxidation of o-diphenols to o-quinones using molecular oxygen, which then polymerizes to form brown or black pigments. The synthesis of o-diphenols is a potentially valuable catalytic ability and thus tyrosinase has attracted a lot of attention with respect to industrial applications. In environmental technology it is used for the detoxification of phenol-containing wastewaters and contaminated soils, as biosensors for phenol monitoring, and for the production of L-DOPA in pharmaceutical industries, and is also used in cosmetic and food industries as important catalytic enzyme. Melanin pigment synthesized by tyrosinase has found applications for protection against radiation cation exchangers, drug carriers, antioxidants, antiviral agents, or immunogen. The recombinant V. spinosum tryosinase protein can be used to produce tailor-made melanin and other polyphenolic materials using various phenols and catechols as starting materials. This review compiles the recent data on biochemical and molecular properties of microbial tyrosinases, underlining their importance in the industrial use of these enzymes. After that, their most promising applications in pharmaceutical, food processing, and environmental fields are presented.

Identifiers

PMID24895537
PMCPMC4033337
OpenAlexW2091854427

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.