Evidence map›Paper›PMID 34062799›Full record

ReviewInternational journal of molecular sciences2021

Laccase and Tyrosinase Biosensors Used in the Determination of Hydroxycinnamic Acids.

Alexandra Virginia Bounegru, Constantin Apetrei

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Electrochemical Sensors for Detection of Phytomolecules: A Mechanistic Approach.Combinatorial chemistry & high throughput screening · 2024
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
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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.

Alexandra Virginia BounegruDepartment of Chemistry, Physics and Environment, Faculty of Sciences and Environment, "Dunărea de Jos" University of Galaţi, 47 Domnească Street, 800008 Galaţi, Romania.ORCID 0000-0002-6005-492X
Constantin ApetreiDepartment of Chemistry, Physics and Environment, Faculty of Sciences and Environment, "Dunărea de Jos" University of Galaţi, 47 Domnească Street, 800008 Galaţi, Romania.ORCID 0000-0002-3823-4174
"Dunarea de Jos" University of Galati · RO

Funding

Romanian Ministry of Education and Research, CNCS-UEFISCDI PN-III-P4-ID-PCE-2020-0923
6 · The paper itself

Abstract

In recent years, researchers have focused on developing simple and efficient methods based on electrochemical biosensors to determine hydroxycinnamic acids from various real samples (wine, beer, propolis, tea, and coffee). Enzymatic biosensors represent a promising, low-cost technology for the direct monitoring of these biologically important compounds, which implies a fast response and simple sample processing procedures. The present review aims at highlighting the structural features of this class of compounds and the importance of hydroxycinnamic acids for the human body, as well as presenting a series of enzymatic biosensors commonly used to quantify these phenolic compounds. Enzyme immobilization techniques on support electrodes are very important for their stability and for obtaining adequate results. The following sections of this review will briefly describe some of the laccase (Lac) and tyrosinase (Tyr) biosensors used for determining the main hydroxycinnamic acids of interest in the food or cosmetics industry. Considering relevant studies in the field, the fact has been noticed that there is a greater number of studies on laccase-based biosensors as compared to those based on tyrosinase for the detection of hydroxycinnamic acids. Significant progress has been made in relation to using the synergy of nanomaterials and nanocomposites for more stable and efficient enzyme immobilization. These nanomaterials are mainly carbon- and/or polymer-based nanostructures and metallic nanoparticles which provide a suitable environment for maintaining the biocatalytic activity of the enzyme and for increasing the rate of electron transport.

Indexed as

Biosensing TechniquesCarbonCoumaric AcidsElectrochemical TechniquesEnzymes, ImmobilizedHumansLaccaseMetal NanoparticlesMonophenol MonooxygenaseCarbonCoumaric AcidsEnzymes, ImmobilizedLaccaseMonophenol Monooxygenasebiosensorenzyme immobilizationhydroxycinnamic acidslaccasetyrosinase

Identifiers

PMID34062799
PMCPMC8125614
OpenAlexW3157180789

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.