Evidence map›Paper›PMID 38461181›Full record

ReviewMolecular biotechnology2025

Abridgement of Microbial Esterases and Their Eminent Industrial Endeavors.

Fatima Akram, Taseer Fatima, Ifrah Shabbir, Ikram Ul Haq, Ramesha Ibrar, Hamid Mukhtar

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.8field-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

7 citing papers in PubMed, 12 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Fatima AkramInstitute of Industrial Biotechnology, Government College University, Lahore, 54000, Pakistan. fatima_iib@yahoo.com.ORCID http://orcid.org/0000-0001-8438-706X
Taseer FatimaInstitute of Industrial Biotechnology, Government College University, Lahore, 54000, Pakistan.
Ifrah ShabbirInstitute of Industrial Biotechnology, Government College University, Lahore, 54000, Pakistan.
Ikram Ul HaqInstitute of Industrial Biotechnology, Government College University, Lahore, 54000, Pakistan.
Ramesha IbrarInstitute of Industrial Biotechnology, Government College University, Lahore, 54000, Pakistan.
Hamid MukhtarInstitute of Industrial Biotechnology, Government College University, Lahore, 54000, Pakistan.
Government College University, Lahore · PKPakistan Academy of Sciences · PK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Esterases are hydrolases that contribute to the hydrolysis of ester bonds into both water-soluble acyl esters and emulsified glycerol-esters containing short-chain acyl groups. They have garnered significant attention from biotechnologists and organic chemists due to their immense commercial value. Esterases, with their diverse and significant properties, have become highly sought after for various industrial applications. Synthesized ubiquitously by a wide range of living organisms, including animals, plants, and microorganisms, these enzymes have found microbial esterases to be the preferred choice in industrial settings. The cost-effective production of microbial esterases ensures higher yields, unaffected by seasonal variations. Their applications span diverse sectors, such as food manufacturing, leather tanneries, paper and pulp production, textiles, detergents, cosmetics, pharmaceuticals, biodiesel synthesis, bioremediation, and waste treatment. As the global trend shifts toward eco-friendly and sustainable practices, industrial processes are evolving with reduced waste generation, lower energy consumption, and the utilization of biocatalysts derived from renewable and unconventional raw materials. This review explores the background, structural characteristics, thermostability, and multifaceted roles of bacterial esterases in crucial industries, aiming to optimize and analyze their properties for continued successful utilization in diverse industrial processes. Additionally, recent advancements in esterase research are overviewed, showcasing novel techniques, innovations, and promising areas for further exploration.

Indexed as

BacteriaBacterial ProteinsBiotechnologyEsterasesEnzyme StabilityHydrolysisBacterial ProteinsEsterasesBacteriaBiocatalystEsteraseHydrolasesThermostable

Identifiers

PMID38461181
OpenAlexW4392618209

What OpenQuestion holds

Textmetadata
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.