Evidence map›Paper›PMID 33481073›Full record

ReviewArchives of microbiology2021

Biosynthesis and industrial applications of α-amylase: a review.

Muhammad Adeel Farooq, Shaukat Ali, Ali Hassan, Hafiz Muhammad Tahir, Samaira Mumtaz, Shumaila Mumtaz

Abstract readReview
PubMed Publisher
In one paragraph

Review in Archives of microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 2 pooled it
16.8field-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

54 citing papers in PubMed, 2 syntheses or guidelines pooled it, 186 citations in OpenAlex.

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  19. Screening for Safe and EfficientFoods (Basel, Switzerland) · 2025
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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 1 institution in 1 country.

Muhammad Adeel FarooqApplied Entomology and Medical Toxicology Laboratory, Department of Zoology, Government College University, Lahore, Pakistan.
Shaukat AliApplied Entomology and Medical Toxicology Laboratory, Department of Zoology, Government College University, Lahore, Pakistan. dr.shaukatali@gcu.edu.pk.ORCID http://orcid.org/0000-0003-2481-1978
Ali HassanApplied Entomology and Medical Toxicology Laboratory, Department of Zoology, Government College University, Lahore, Pakistan.
Hafiz Muhammad TahirApplied Entomology and Medical Toxicology Laboratory, Department of Zoology, Government College University, Lahore, Pakistan.
Samaira MumtazApplied Entomology and Medical Toxicology Laboratory, Department of Zoology, Government College University, Lahore, Pakistan.
Shumaila MumtazApplied Entomology and Medical Toxicology Laboratory, Department of Zoology, Government College University, Lahore, Pakistan.
Government College University, Lahore · PK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amylase is amongst the most indispensable enzymes that have a large number of applications in laboratories and industries. Mostly, α-amylase is synthesized from microbes such as bacteria, fungi and yeast. Due to the high demand for α-amylase, its synthesis can be enhanced using recombinant DNA technology, different fermentation methods, less expensive and good carbon and nitrogen sources, and optimizing the various parameters during fermentation, e.g., temperature, pH and fermentation duration. Various methods are used to measure the production and activity of synthesized α-amylase like iodine, DNS, NS and dextrinizing methods. The activity of crude α-amylase can be elevated to the maximum level by optimizing the temperature and pH. Some metals also interact with α-amylase and increase its activity like K

Indexed as

alpha-AmylasesBacteriaCarbonFermentationFungiHydrogen-Ion ConcentrationIndustryMetalsNitrogenRecombinant ProteinsTemperaturealpha-AmylasesCarbonMetalsNitrogenRecombinant ProteinsApplicationFermentationMicrobesParametersα-amylase

Identifiers

PMID33481073
OpenAlexW3125352898

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.