Evidence map›Paper›PMID 39452849›Full record

ReviewMarine drugs2024

Plastic-Degrading Enzymes from Marine Microorganisms and Their Potential Value in Recycling Technologies.

Robert Ruginescu, Cristina Purcarea

Abstract readReview
In one paragraph

Review in Marine drugs, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
–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

8 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. The effect of ionic strength on PETase enzymes: An experimental and computational study.Protein science : a publication of the Protein Society · 2026
    Article
  5. Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026
    Article
  6. Article
  7. Review
  8. 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

2 authors.

Robert RuginescuDepartment of Microbiology, Institute of Biology Bucharest of the Romanian Academy, 296 Splaiul Independentei, 060031 Bucharest, Romania.ORCID 0000-0002-0461-1437
Cristina PurcareaDepartment of Microbiology, Institute of Biology Bucharest of the Romanian Academy, 296 Splaiul Independentei, 060031 Bucharest, Romania.ORCID 0000-0001-5784-8545

Funding

Romanian Academy RO1567-IBB05/2024
6 · The paper itself

Abstract

Since the 2005 discovery of the first enzyme capable of depolymerizing polyethylene terephthalate (PET), an aromatic polyester once thought to be enzymatically inert, extensive research has been undertaken to identify and engineer new biocatalysts for plastic degradation. This effort was directed toward developing efficient enzymatic recycling technologies that could overcome the limitations of mechanical and chemical methods. These enzymes are versatile molecules obtained from microorganisms living in various environments, including soil, compost, surface seawater, and extreme habitats such as hot springs, hydrothermal vents, deep-sea regions, and Antarctic seawater. Among various plastics, PET and polylactic acid (PLA) have been the primary focus of enzymatic depolymerization research, greatly enhancing our knowledge of enzymes that degrade these specific polymers. They often display unique catalytic properties that reflect their particular ecological niches. This review explores recent advancements in marine-derived enzymes that can depolymerize synthetic plastic polymers, emphasizing their structural and functional features that influence the efficiency of these catalysts in biorecycling processes. Current status and future perspectives of enzymatic plastic depolymerization are also discussed, with a focus on the underexplored marine enzymatic resources.

Indexed as

Aquatic OrganismsPlasticsBiocatalysisBiodegradation, EnvironmentalEnzymesPolyestersPolyethylene TerephthalatesRecyclingSeawaterEnzymesPlasticsPolyestersPolyethylene TerephthalatescutinaseesterasePET hydrolasesPLA biodegradationsynthetic polymers

Identifiers

PMID39452849
PMCPMC11509169

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.