Evidence map›Paper›PMID 25207718›Full record

ReviewMolecules (Basel, Switzerland)2014

Inorganic materials as supports for covalent enzyme immobilization: methods and mechanisms.

Paolo Zucca, Enrico Sanjust

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
11.7field-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

76 citing papers in PubMed, 461 citations in OpenAlex.

  1. Article
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  10. An Organic Solvent-Tolerant α-L-Rhamnosidase fromMolecules (Basel, Switzerland) · 2025
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  15. Recombinant Esterase (BaCEApplied biochemistry and biotechnology · 2025
    Article
  16. Preparation and Biochemical Characterization ofMolecules (Basel, Switzerland) · 2025
    Article
  17. Review
  18. Review
  19. Article
  20. Article

16 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

2 authors at 1 institution in 1 country.

Paolo ZuccaConsorzio UNO, Consortium University of Oristano, Oristano 09170, Italy. pzucca@unica.it.
Enrico SanjustDipartimento di Scienze Biomediche, Università di Cagliari, Monserrato 09042, Italy. sanjust@unica.it.
Fondazione Centro Marino Internazionale · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several inorganic materials are potentially suitable for enzymatic covalent immobilization, by means of several different techniques. Such materials must meet stringent criteria to be suitable as solid matrices: complete insolubility in water, reasonable mechanical strength and chemical resistance under the operational conditions, the capability to form manageable particles with high surface area, reactivity towards derivatizing/functionalizing agents. Non-specific protein adsorption should be always considered when planning covalent immobilization on inorganic solids. A huge mass of experimental work has shown that silica, silicates, borosilicates and aluminosilicates, alumina, titania, and other oxides, are the materials of choice when attempting enzyme immobilizations on inorganic supports. More recently, some forms of elemental carbon, silicon, and certain metals have been also proposed for certain applications. With regard to the derivatization/functionalization techniques, the use of organosilanes through silanization is undoubtedly the most studied and the most applied, although inorganic bridge formation and acylation with selected acyl halides have been deeply studied. In the present article, the most common inorganic supports for covalent immobilization of the enzymes are reviewed, with particular focus on their advantages and disadvantages in terms of enzyme loadings, operational stability, undesired adsorption, and costs. Mechanisms and methods for covalent immobilization are also discussed, focusing on the most widespread activating approaches (such as glutaraldehyde, cyanogen bromide, divinylsulfone, carbodiimides, carbonyldiimidazole, sulfonyl chlorides, chlorocarbonates, N-hydroxysuccinimides).

Indexed as

AdsorptionCross-Linking ReagentsEnzymes, ImmobilizedHydrocarbons, HalogenatedProtein BindingSilicon DioxideSurface PropertiesCross-Linking ReagentsEnzymes, ImmobilizedHydrocarbons, HalogenatedSilicon Dioxide

Identifiers

PMID25207718
PMCPMC6272024
OpenAlexW2036929504

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.