Evidence map›Paper›PMID 39125688›Full record

ArticleInternational journal of molecular sciences2024

Biochemical Characterisation of Sis: A Distinct Thermophilic PETase with Enhanced NanoPET Substrate Hydrolysis and Thermal Stability.

Carmen Ercolano, Roberta Iacono, Valeria Cafaro, Elio Pizzo, Donato Giovannelli, Golo Feuerriegel, Wolfgang R Streit, Andrea Strazzulli, Marco Moracci

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025
    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

9 authors.

Carmen ErcolanoDepartment of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy.
Roberta IaconoDepartment of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy.ORCID 0000-0002-3586-4322
Valeria CafaroDepartment of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy.ORCID 0000-0002-6686-7657
Elio PizzoDepartment of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy.ORCID 0000-0002-3652-8865
Donato GiovannelliDepartment of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy.
Golo FeuerriegelDepartment of Microbiology and Biotechnology, University of Hamburg, 22609 Hamburg, Germany.ORCID 0000-0003-0741-1729
Wolfgang R StreitDepartment of Microbiology and Biotechnology, University of Hamburg, 22609 Hamburg, Germany.
Andrea StrazzulliDepartment of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy.ORCID 0000-0002-9690-149X
Marco MoracciDepartment of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy.ORCID 0000-0002-9846-2531

Funding

Ministero dell'Università e della Ricerca (MUR) 2020SBNHLH_003
6 · The paper itself

Abstract

Polyethylene terephthalate (PET) degradation by enzymatic hydrolysis is significant for addressing plastic pollution and fostering sustainable waste management practices. Identifying thermophilic and thermostable PET hydrolases is particularly crucial for industrial bioprocesses, where elevated temperatures may enhance enzymatic efficiency and process kinetics. In this study, we present the discovery of a novel thermophilic and thermostable PETase enzyme named Sis, obtained through metagenomic sequence-based analysis. Sis exhibits robust activity on nanoPET substrates, demonstrating effectiveness at temperatures up to 70 °C and displaying exceptional thermal stability with a melting temperature (T

Indexed as

Enzyme StabilityPolyethylene TerephthalatesBacterial ProteinsHydrolasesHydrolysisKineticsPhylogenySubstrate SpecificityTemperatureBacterial ProteinsHydrolasesPolyethylene Terephthalatesenzyme discoveryPET hydrolysisthermozymes

Identifiers

PMID39125688
PMCPMC11311821

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.