Evidence map›Paper›PMID 24980481›Full record

ArticleJournal of colloid and interface science2014

Immobilization of glucose oxidase to nanostructured films of polystyrene-block-poly(2-vinylpyridine).

Samir A Bhakta, Tomas E Benavidez, Carlos D Garcia

Open access · bronzeAbstract read
In one paragraph

Article in Journal of colloid and interface science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

  1. In-situ Neutron Reflectometry Study on Adsorption of Glucose Oxidase at Mesoporous Aluminum Oxide Film.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2020
    Article
  2. Article
  3. Article
  4. 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

3 authors at 1 institution in 1 country.

Samir A BhaktaDepartment of Chemistry, The University of Texas at San Antonio One UTSA Circle, San Antonio, TX 78249, USA.
Tomas E BenavidezDepartment of Chemistry, The University of Texas at San Antonio One UTSA Circle, San Antonio, TX 78249, USA.
Carlos D GarciaDepartment of Chemistry, The University of Texas at San Antonio One UTSA Circle, San Antonio, TX 78249, USA. Electronic address: carlos.garcia@utsa.edu.
The University of Texas at San Antonio · US

Funding

RCMI Center for Interdiscplinary Health Research CIHRG12MD007591 · NIMHD · UNIVERSITY OF TEXAS SAN ANTONIO · PI PERRY, GEORGE · 2012 to 2016
$10.4M
UNDERSTANDING THE INTERACTION OF ANKYRINS AND NANOMATERIALSSC3GM081085 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI GARCIA, CARLOS DIEGO · 2007 to 2015
$844k
NIGMS NIH HHS 1SC3GM081085NIGMS NIH HHS 2SC3GM081085NIGMS NIH HHS SC3 GM081085NIMHD NIH HHS G12 MD007591NIMHD NIH HHS G12MD007591
6 · The paper itself

Abstract

A critical step for the development of biosensors is the immobilization of the biorecognition element to the surface of a substrate. Among other materials that can be used as substrates, block copolymers have the untapped potential to provide significant advantages for the immobilization of proteins. To explore such possibility, this manuscript describes the fabrication and characterization of thin-films of polystyrene-block-poly(2-vinylpyridine) (PS-b-P2VP). These films were then used to investigate the immobilization of glucose oxidase, a model enzyme for the development of biosensors. According to the results presented, the nanoporous films can provide significant increases in surface area of the substrate and the immobilization of larger amounts of active enzyme. The characterization of the substrate-enzyme interface discussed in the manuscript aims to provide critical information about relationship between the surface (material, geometry, and density of pores), the protein structure, and the immobilization conditions (pH, and protein concentration) required to improve the catalytic activity and stability of the enzymes. A maximum normalized activity of 3300±700 U m(-2) was achieved for the nanoporous film of PS-b-P2VP.

Indexed as

Biosensing TechniquesMembranes, ArtificialEnzymes, ImmobilizedGlucose OxidaseNanostructuresPolystyrenesPolyvinylsPorosityPyridinesEnzymes, ImmobilizedGlucose OxidaseMembranes, Artificialpolystyrene-block-poly(2-vinylpyridine)PolystyrenesPolyvinylsPyridinesAdsorptionAtomic force microscopyEllipsometryEntrapmentGlucose oxidaseNanoporous materialsPolystyrene-block-poly(2-vinylpyridine)

Identifiers

PMID24980481
PMCPMC4131735
OpenAlexW2024299084

What OpenQuestion holds

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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.