Evidence map›Paper›PMID 38474502›Full record

ReviewMolecules (Basel, Switzerland)2024

Enzymes in "Green" Synthetic Chemistry: Laccase and Lipase.

Dieter M Scheibel, Ioan Pavel Ivanov Gitsov, Ivan Gitsov

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
24.6field-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

18 citing papers in PubMed, 41 citations in OpenAlex.

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  17. Ganodermataceae-current status, research, and development in Lower Mekong Basin.Frontiers in cellular and infection microbiology · 2025
    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

3 authors at 1 institution in 1 country.

Dieter M ScheibelDepartment of Chemistry, State University of New York-ESF, Syracuse, NY 13210, USA.
Ioan Pavel Ivanov GitsovScience and Technology, Medtronic Incorporated, 710 Medtronic Parkway, Minneapolis, MN 55432, USA.ORCID 0009-0001-7030-8153
Ivan GitsovDepartment of Chemistry, State University of New York-ESF, Syracuse, NY 13210, USA.ORCID 0000-0001-7433-8571
State University of New York · US

Funding

Syracuse University 1168699-1-8709
6 · The paper itself

Abstract

Enzymes play an important role in numerous natural processes and are increasingly being utilized as environmentally friendly substitutes and alternatives to many common catalysts. Their essential advantages are high catalytic efficiency, substrate specificity, minimal formation of byproducts, and low energy demand. All of these benefits make enzymes highly desirable targets of academic research and industrial development. This review has the modest aim of briefly overviewing the classification, mechanism of action, basic kinetics and reaction condition effects that are common across all six enzyme classes. Special attention is devoted to immobilization strategies as the main tools to improve the resistance to environmental stress factors (temperature, pH and solvents) and prolong the catalytic lifecycle of these biocatalysts. The advantages and drawbacks of methods such as macromolecular crosslinking, solid scaffold carriers, entrapment, and surface modification (covalent and physical) are discussed and illustrated using numerous examples. Among the hundreds and possibly thousands of known and recently discovered enzymes, hydrolases and oxidoreductases are distinguished by their relative availability, stability, and wide use in synthetic applications, which include pharmaceutics, food and beverage treatments, environmental clean-up, and polymerizations. Two representatives of those groups-laccase (an oxidoreductase) and lipase (a hydrolase)-are discussed at length, including their structure, catalytic mechanism, and diverse usage. Objective representation of the current status and emerging trends are provided in the main conclusions.

Indexed as

LaccaseLipaseCatalysisEnzymes, ImmobilizedMacromolecular SubstancesEnzymes, ImmobilizedLaccaseLipaseMacromolecular Substancesenzymes“green” chemistryimmobilizationlaccaselinear-dendritic copolymerslipasepolymerizationpolyphenolswine making

Identifiers

PMID38474502
PMCPMC10934700
OpenAlexW4392154427

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.