ArticleJournal of industrial microbiology & biotechnology2012
Cloning and characterization of two new thermostable and alkalitolerant α-amylases from the Anoxybacillus species that produce high levels of maltose.
Article in Journal of industrial microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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.
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.
Who cites it
24 citing papers in PubMed, 62 citations in OpenAlex.
- The role of N185D substitution in enhancing activity of BaqA∆C α-amylase.Scientific reports · 2025Article
- Probing the function of C-terminal region of recombinant α-amylase BmaN1 fromMicrobiology spectrum · 2024Article
- Phylogenomic and molecular marker based studies to clarify the evolutionary relationships amongstInternational journal of systematic and evolutionary microbiology · 2024Article
- Article
- Detergent-resistant α-amylase derived from Anoxybacillus karvacharensis K1 and its production based on whey.Scientific reports · 2024Article
- The genus Anoxybacillus: an emerging and versatile source of valuable biotechnological products.Extremophiles : life under extreme conditions · 2023Review
- Anoxybacillus: an overview of a versatile genus with recent biotechnological applications.World journal of microbiology & biotechnology · 2023Review
- Biochemical and synergistic properties of a novel alpha-amylase from Chinese nong-flavor Daqu.Microbial cell factories · 2021Article
- A Novel Digestive α-Amylase from Blue Crab (International journal of molecular sciences · 2021Article
- Colombian Andean thermal springs: reservoir of thermophilic anaerobic bacteria producing hydrolytic enzymes.Extremophiles : life under extreme conditions · 2019Article
- Influence of Calcium Ions on the Thermal Characteristics of α-amylase from Thermophilic Anoxybacillus sp. GXS-BL.Protein and peptide letters · 2019Article
- Introduction of novel thermostable α-amylases from genus Anoxybacillus and proposing to group the Bacillaceae related α-amylases under five individual GH13 subfamilies.World journal of microbiology & biotechnology · 2018Article
- Article
- A new group of glycoside hydrolase family 13 α-amylases with an aberrant catalytic triad.Scientific reports · 2017Article
- Immobilization of α-Amylase from Anoxybacillus sp. SK3-4 on ReliZyme and Immobead Supports.Molecules (Basel, Switzerland) · 2016Article
- Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass.Scientific reports · 2016Article
- Purification and Characterization of Thermostable and Detergent-Stable α-Amylase fromFood technology and biotechnology · 2016Article
- Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications.Frontiers in microbiology · 2016Review
- Genome sequence of Anoxybacillus ayderensis AB04(T) isolated from the Ayder hot spring in Turkey.Standards in genomic sciences · 2015Article
- Protein engineering of selected residues from conserved sequence regions of a novel Anoxybacillus α-amylase.Scientific reports · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two genes that encode α-amylases from two Anoxybacillus species were cloned and expressed in Escherichia coli. The genes are 1,518 bp long and encode 506 amino acids. Both sequences are 98% similar but are distinct from other well-known α-amylases. Both of the recombinant enzymes, ASKA and ADTA, were purified using an α-CD-Sepharose column. They exhibited an optimum activity at 60°C and pH 8. Both amylases were stable at pH 6-10. At 60°C in the absence of Ca²⁺, negligible reduction in activity for up to 48 h was observed. The activity half-life at 65°C was 48 and 3 h for ASKA and ADTA, respectively. In the presence of Ca²⁺ ions, both amylases were highly stable for at least 48 h and had less than a 10% decrease in activity at 70°C. Both enzymes exhibited similar end-product profiles, and the predominant yield was maltose (69%) from starch hydrolysis. To the best of our knowledge, most α-amylases that produce high levels of maltose are active at an acidic to neutral pH. This is the first report of two thermostable, alkalitolerant recombinant α-amylases from Anoxybacillus that produce high levels of maltose and have an atypical protein sequence compared with known α-amylases.
Indexed as
Identifiers
What OpenQuestion holds
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.