ReviewFrontiers in bioengineering and biotechnology2018
An Insight Into Ameliorating Production, Catalytic Efficiency, Thermostability and Starch Saccharification of Acid-Stable α-Amylases From Acidophiles.
Review in Frontiers in bioengineering and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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.
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Who cites it
14 citing papers in PubMed, 40 citations in OpenAlex.
- α-Amylase: Its Structure, Molecular Modification, and Application in the Food Field.Foods (Basel, Switzerland) · 2026Review
- Enhancing stability of enzymes for industrial applications: molecular insights and emerging approaches.World journal of microbiology & biotechnology · 2025Review
- Article
- Enhanced saccharification levels of corn starch using as a strategy a novel amylolytic complex (AmyHb) from the thermophilic fungus3 Biotech · 2024Article
- Acid-resistant enzymes: the acquisition strategies and applications.Applied microbiology and biotechnology · 2023Review
- Optimization of amylase production using response surface methodology from newly isolated thermophilic bacteria.Heliyon · 2023Article
- Microreactor equipped with naturally acid-resistant histidine ammonia lyase from an extremophile.Materials advances · 2022Article
- Structural and functional adaptation in extremophilic microbial α-amylases.Biophysical reviews · 2022Review
- Prediction and Inferred Evolution of Acid Tolerance Genes in the Biotechnologically ImportantFrontiers in microbiology · 2022Article
- Characterization of redox and salinity-tolerant alkaline protease fromFrontiers in microbiology · 2022Article
- Industrial Biotechnology Based on Enzymes From Extreme Environments.Frontiers in bioengineering and biotechnology · 2022Review
- Improvement of thermostability and catalytic efficiency of glucoamylase from Talaromyces leycettanus JCM12802 via site-directed mutagenesis to enhance industrial saccharification applications.Biotechnology for biofuels · 2021Article
- Molecular strategies to enhance stability and catalysis of extremophile-derived α-amylase using computational biology.Extremophiles : life under extreme conditions · 2021Review
- Activity-Based Protein Profiling of Retaining α-Amylases in Complex Biological Samples.Journal of the American Chemical Society · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most of the extracellular enzymes of acidophilic bacteria and archaea are stable at acidic pH with a relatively high thermostability. There is, however, a dearth of information on their acid stability. Although several theories have been postulated, the adaptation of acidophilic proteins to low pH has not been explained convincingly. This review highlights recent developments in understanding the structure and biochemical characteristics, and production of acid-stable and calcium-independent α-amylases by acidophilic bacteria with special reference to that of
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Registered trials
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.