ArticleInternational journal of molecular sciences2013
A high molecular-mass Anoxybacillus sp. SK3-4 amylopullulanase: characterization and its relationship in carbohydrate utilization.
Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 35 citations in OpenAlex.
- Microbial diversity and metabolic predictions of high-temperature streamer biofilms using metagenome-assembled genomes.Scientific reports · 2025Article
- The genus Anoxybacillus: an emerging and versatile source of valuable biotechnological products.Extremophiles : life under extreme conditions · 2023Review
- Biotechnology and bioengineering of pullulanase: state of the art and perspectives.World journal of microbiology & biotechnology · 2021Review
- Whole-Genome Sequence Data Analysis ofBioMed research international · 2021Article
- Identification of proteins associated with pediatric bilateral Wilms tumor.Oncology letters · 2016Article
- Characterization of the starch-acting MaAmyB enzyme from Microbacterium aurum B8.A representing the novel subfamily GH13_42 with an unusual, multi-domain organization.Scientific reports · 2016Article
- Immobilization of α-Amylase from Anoxybacillus sp. SK3-4 on ReliZyme and Immobead Supports.Molecules (Basel, Switzerland) · 2016Article
- Structure and function of α-glucan debranching enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass.Scientific reports · 2016Article
- Improving the Thermostability of Acidic Pullulanase from Bacillus naganoensis by Rational Design.PloS one · 2016Article
- Genome Sequence of Anoxybacillus geothermalis Strain GSsed3, a Novel Thermophilic Endospore-Forming Species.Genome announcements · 2015Article
- 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
- Analysis of anoxybacillus genomes from the aspects of lifestyle adaptations, prophage diversity, and carbohydrate metabolism.PloS one · 2014Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
An amylopullulanase of the thermophilic Anoxybacillus sp. SK3-4 (ApuASK) was purified to homogeneity and characterized. Though amylopullulanases larger than 200 kDa are rare, the molecular mass of purified ApuASK appears to be approximately 225 kDa, on both SDS-PAGE analyses and native-PAGE analyses. ApuASK was stable between pH 6.0 and pH 8.0 and exhibited optimal activity at pH 7.5. The optimal temperature for ApuASK enzyme activity was 60 °C, and it retained 54% of its total activity for 240 min at 65 °C. ApuASK reacts with pullulan, starch, glycogen, and dextrin, yielding glucose, maltose, and maltotriose. Interestingly, most of the previously described amylopullulanases are unable to produce glucose and maltose from these substrates. Thus, ApuASK is a novel, high molecular-mass amylopullulanase able to produce glucose, maltose, and maltotriose from pullulan and starch. Based on whole genome sequencing data, ApuASK appeared to be the largest protein present in Anoxybacillus sp. SK3-4. The α-amylase catalytic domain present in all of the amylase superfamily members is present in ApuASK, located between the cyclodextrin (CD)-pullulan-degrading N-terminus and the α-amylase catalytic C-terminus (amyC) domains. In addition, the existence of a S-layer homology (SLH) domain indicates that ApuASK might function as a cell-anchoring enzyme and be important for carbohydrate utilization in a streaming hot spring.
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