Evidence map›Paper›PMID 27869778›Full record

ReviewMolecules (Basel, Switzerland)2016

Agarose and Its Derivatives as Supports for Enzyme Immobilization.

Paolo Zucca, Roberto Fernandez-Lafuente, Enrico Sanjust

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
13.2field-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

67 citing papers in PubMed, 308 citations in OpenAlex.

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7 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.

Paolo ZuccaDipartimento di Scienze Biomediche, Università di Cagliari, 09042 Monserrato (CA), Italy. pzucca@unica.it.
Roberto Fernandez-LafuenteDepartamento de Biocatalisis, ICP-CSIC; C/Marie Curie 2, Campus UAM-CSIC, Madrid 28049, Spain. rfl@icp.csic.es.
Enrico SanjustDipartimento di Scienze Biomediche, Università di Cagliari, 09042 Monserrato (CA), Italy. sanjust@unica.it.
Consejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Agarose is a polysaccharide obtained from some seaweeds, with a quite particular structure that allows spontaneous gelation. Agarose-based beads are highly porous, mechanically resistant, chemically and physically inert, and sharply hydrophilic. These features-that could be further improved by means of covalent cross-linking-render them particularly suitable for enzyme immobilization with a wide range of derivatization methods taking advantage of chemical modification of a fraction of the polymer hydroxyls. The main properties of the polymer are described here, followed by a review of cross-linking and derivatization methods. Some recent, innovative procedures to optimize the catalytic activity and operational stability of the obtained preparations are also described, together with multi-enzyme immobilized systems and the main guidelines to exploit their performances.

Indexed as

AgarEnzymes, ImmobilizedEnzyme StabilityImmobilizationSepharoseAgarEnzymes, ImmobilizedSepharoseagar-agaragarosecross-linkingenzymesfunctionalizationimmobilizationstabilization

Identifiers

PMID27869778
PMCPMC6273708
OpenAlexW2555005084

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.