Evidence map›Paper›PMID 33754213›Full record

ReviewExtremophiles : life under extreme conditions2021

Molecular strategies to enhance stability and catalysis of extremophile-derived α-amylase using computational biology.

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

Abstract readReview
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In one paragraph

Review in Extremophiles : life under extreme conditions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

2 citing papers in PubMed, 16 citations in OpenAlex.

  1. Computational design of α-amylase fromComputational and structural biotechnology journal · 2024
    Article
  2. Article
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.

Nisha Gupta *School of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India.
Esmil Beliya *School of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India.
Jai Shankar PaulSchool of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India. jaishankar_paul@yahoo.com.
Shubhra TiwariSchool of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India.
Shriram KunjamDepartment of Botany, Govt. VYPT PG Autonomous College, Durg, CG, 491001, India.
Shailesh Kumar JadhavSchool of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, CG, 492010, India.
Pandit Ravishankar Shukla University · INGovernment Medical College · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Amylase is the most significant glycoside hydrolase having applications in various industries. It cleaves the α,1-4 glucosidic linkages of polysaccharides like starch, glycogen to yield a small polymer of glucose in α-anomeric configuration. α-Amylase is produced by all the three domains of life but microorganisms are preferred sources for industrial-scale production due to several advantages. Enormous studies and research have been done in this field in the past few decades. Still, it is requisite to work on enzyme stability and catalysis, as it loses its functionality in extreme. As the enzyme loses its structural and catalytic property under extreme environmental conditions, it is mandatory to confer some potential strategies for enhancing enzyme behaviour in such conditions. This limitation of an enzyme can be overcome up to some extent by extremophiles. They serve as an excellent source of α-amylase with outstanding features. This review is an attempt to encapsulate some structure-based strategies for improving enzyme behaviour thereby enabling researchers to selectively amend any of the strategies as per requirement during upstream and downstream processing for higher enzyme yield and stability. Thus, it will provide some cutting-edge strategies for tailoring α-amylase producing organism and enzyme with the help of several computational biology tools.

Indexed as

alpha-AmylasesExtremophilesAmylasesCatalysisComputational Biologyalpha-AmylasesAmylasesComputational biologyExtremophilesGlycoside hydrolaseStructural insightsα-Amylase

Identifiers

PMID33754213
OpenAlexW3139176459

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.