Evidence map›Paper›PMID 34648116›Full record

ReviewApplied biochemistry and biotechnology2021

Understanding the Basis of Occurrence, Biosynthesis, and Implications of Thermostable Alkaline Proteases.

Prashant S Arya, Shivani M Yagnik, Kiransinh N Rajput, Rakeshkumar R Panchal, Vikram H Raval

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 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Review
  2. Thermostable Proteases fromMicroorganisms · 2025
    Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. 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

5 authors.

Prashant S AryaDepartment of Microbiology and Biotechnology, School of Sciences, Gujarat University, Ahmedabad, 380009, India.
Shivani M YagnikDepartment of Microbiology and Biotechnology, School of Sciences, Gujarat University, Ahmedabad, 380009, India.
Kiransinh N RajputDepartment of Microbiology and Biotechnology, School of Sciences, Gujarat University, Ahmedabad, 380009, India.
Rakeshkumar R PanchalDepartment of Microbiology and Biotechnology, School of Sciences, Gujarat University, Ahmedabad, 380009, India.
Vikram H RavalDepartment of Microbiology and Biotechnology, School of Sciences, Gujarat University, Ahmedabad, 380009, India. vhraval@gujaratuniversity.ac.in.

Funding

Department of Higher Education, Government of Gujarat SHODH - ScHeme of Developing High-Quality Research 201901380034University Grants Commission UGC-BSR Start-Up Research Grant No.F.30-521/2020
6 · The paper itself

Abstract

The group of hydrolytic enzymes synonymously known as proteases is predominantly most favored for the class of industrial enzymes. The present work focuses on the thermostable nature of these proteolytic enzymes that occur naturally among mesophilic and thermophilic microbes. The broad thermo-active feature (40-80 °C), ease of cultivation, maintenance, and bulk production are the key features associated with these enzymes. Detailing of contemporary production technologies, and controllable operational parameters including the purification strategies, are the key features that justify their industrial dominance as biocatalysts. In addition, the rigorous research inputs by protein engineering and enzyme immobilization studies add up to the thermo-catalytic features and application capabilities of these enzymes. The work summarizes key features of microbial proteases that make them numero-uno for laundry, biomaterials, waste management, food and feed, tannery, and medical as well as pharmaceutical industries. The quest for novel and/or designed and engineered thermostable protease from unexplored sources is highly stimulating and will address the ever-increasing industrial demands.

Indexed as

Cysteine EndopeptidasesHot TemperatureProtein EngineeringEnzyme StabilityHydrolysisalkaline peptidaseCysteine EndopeptidasesFermentationImmobilizationIndustrial applicationsProtein engineeringPurificationThermostable proteases

Identifiers

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.