Evidence map›Paper›PMID 36614271›Full record

ArticleInternational journal of molecular sciences2023

Triggering of Polymer-Degrading Enzymes from Layered Double Hydroxides for Recycling Strategies.

Angela Romano, Antonella Rosato, Stefano Bianchi, Giulio Zanaroli, Annamaria Celli, Grazia Totaro, Laura Sisti

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. 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
0.7field-weighted citation impact, top 39% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

  1. 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

7 authors at 1 institution in 1 country.

Angela RomanoDipartimento di Ingegneria Civile, Chimica, Ambientale e dei Materiali, Università di Bologna, Via Terracini 28, 40131 Bologna, Italy.
Antonella RosatoDipartimento di Ingegneria Civile, Chimica, Ambientale e dei Materiali, Università di Bologna, Via Terracini 28, 40131 Bologna, Italy.
Stefano BianchiDipartimento di Ingegneria Civile, Chimica, Ambientale e dei Materiali, Università di Bologna, Via Terracini 28, 40131 Bologna, Italy.
Giulio ZanaroliDipartimento di Ingegneria Civile, Chimica, Ambientale e dei Materiali, Università di Bologna, Via Terracini 28, 40131 Bologna, Italy.
Annamaria CelliDipartimento di Ingegneria Civile, Chimica, Ambientale e dei Materiali, Università di Bologna, Via Terracini 28, 40131 Bologna, Italy.ORCID 0000-0002-5974-1642
Grazia TotaroDipartimento di Ingegneria Civile, Chimica, Ambientale e dei Materiali, Università di Bologna, Via Terracini 28, 40131 Bologna, Italy.ORCID 0000-0002-7388-8894
Laura SistiDipartimento di Ingegneria Civile, Chimica, Ambientale e dei Materiali, Università di Bologna, Via Terracini 28, 40131 Bologna, Italy.ORCID 0000-0003-4445-3880
University of Bologna · IT

Funding

European Union, Horizon 2020; Terminus project European Union, Horizon 2020; Terminus project
6 · The paper itself

Abstract

The use of degrading enzymes in polymer formulation is a very attractive strategy to manage the end-of-life of plastics. However, high temperatures cause the denaturation of enzymes and the loss of their catalytic activity; therefore, protection strategies are necessary. Once protected, the enzyme needs to be released in appropriate media to exert its catalytic activity. A successful protection strategy involves the use of layered double hydroxides: cutinase, selected as a highly degrading polyester hydrolytic enzyme, is thermally protected by immobilization in Mg/Al layered double hydroxide structures. Different triggering media are here evaluated in order to find the best releasing conditions of cutinase from LDH. In detail, phosphate and citrate-phosphate buffers, potassium carbonate, sodium chloride, and sodium sulfate solutions are studied. After the comparison of all media in terms of protein release and activity retained, phosphate buffer is selected as the best candidate for the release of cutinase from LDH, and the effect of pH and concentration is also evaluated. The amount of the enzyme released is determined with the Lowry method. Activity tests are performed via spectrophotometry.

Indexed as

HydroxidesPolymersPhosphatesHydroxidesPhosphatesPolymersenzyme triggeringmultilayer recyclingpolymer-degrading enzyme

Identifiers

PMID36614271
PMCPMC9821672
OpenAlexW4313516608

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.