Evidence map›Paper›PMID 33715051›Full record

ReviewApplied biochemistry and biotechnology2021

Aspects and Recent Trends in Microbial α-Amylase: a Review.

Jai Shankar Paul, Nisha Gupta, Esmil Beliya, Shubhra Tiwari, Shailesh Kumar Jadhav

Abstract readReview
PubMed Publisher
In one paragraph

Review in Applied biochemistry and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
11.9field-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

40 citing papers in PubMed, 131 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

5 authors at 2 institutions in 1 country.

Jai Shankar PaulSchool of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India.
Nisha GuptaSchool of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India.
Esmil BeliyaSchool of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India.
Shubhra TiwariSchool of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India.
Shailesh Kumar JadhavSchool of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India. jadhav9862@gmail.com.
Pandit Ravishankar Shukla University · INGovernment Medical College · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Amylases are the oldest and versatile starch hydrolysing enzymes which can replace chemical hydrolysis of starch in industries. It cleaves the α-(1,4)-D-glucosidic linkage of starch and other related polysaccharides to yield simple sugars like glucose, maltose and limit dextrin. α-Amylase covers about 30% shares of the total enzyme market. On account of their superior features, α-amylase is the most widely used among all the existing amylases for hydrolysis of polysaccharides. Endo-acting α-amylase of glycoside hydrolase family 13 is an extensively used biocatalyst and has various biotechnological applications like in starch processing, detergent, textile, paper and pharmaceutical industries. Apart from these, it has some novel applications including polymeric material for drug delivery, bioremediating agent, biodemulsifier and biofilm inhibitor. The present review will accomplish the research gap by providing the unexplored aspects of microbial α-amylase. It will allow the readers to know about the works that have already been done and the latest trends in this field. The manuscript has covered the latest immobilization techniques and the site-directed mutagenesis approaches which are readily being performed to confer the desirable property in wild-type α-amylases. Furthermore, it will state the inadequacies and the numerous obstacles coming in the way of its production during upstream and downstream steps and will also suggest some measures to obtain stable and industrial-grade α-amylase.

Indexed as

Biotechnologyalpha-AmylasesStarchalpha-AmylasesStarchBiocatalystDrug deliveryGlycoside hydrolasesGlycosidic linkageα-Amylase

Identifiers

PMID33715051
OpenAlexW3136882533

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.