ArticleJournal of microbiology (Seoul, Korea)2017
The hyperthermophilic α-amylase from Thermococcus sp. HJ21 does not require exogenous calcium for thermostability because of high-binding affinity to calcium.
Article in Journal of microbiology (Seoul, Korea), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.
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Who cites it
5 citing papers in PubMed, 1 synthesis or guideline pooled it, 14 citations in OpenAlex.
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Structural and functional adaptation in extremophilic microbial α-amylases.Biophysical reviews · 2022Review
- Biochemical and synergistic properties of a novel alpha-amylase from Chinese nong-flavor Daqu.Microbial cell factories · 2021Article
- A new GH13 subfamily represented by the α-amylase from the halophilic archaeon Haloarcula hispanica.Extremophiles : life under extreme conditions · 2020Article
- Functional and cooperative stabilization of a two-metal (Ca, Zn) center in α-amylase derived from Flavobacteriaceae species.Scientific reports · 2017Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
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Abstract
The hyperthermophilic α-amylase from Thermococcus sp. HJ21 does not require exogenous calcium ions for thermostability, and is a promising alternative to commercially available α-amylases to increase the efficiency of industrial processes like the liquefaction of starch. We analyzed the amino acid sequence of this α-amylase by sequence alignments and structural modeling, and found that this α-amylase closely resembles the α-amylase from Pyrococcus woesei. The gene of this α-amylase was cloned in Escherichia coli and the recombinant α-amylase was overexpressed and purified with a combined renaturation-purification procedure. We confirmed thermostability and exogenous calcium ion independency of the recombinant α-amylase and further investigated the mechanism of the independency using biochemical approaches. The results suggested that the α-amylase has a high calcium ion binding affinity that traps a calcium ion that would not dissociate at high temperatures, providing a direct explanation as to why the addition of calcium ions is not required for thermostability. Understanding of the mechanism offers a strong base on which to further engineer properties of this α-amylase for better potential applications in industrial processes.
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