ArticleBMC biotechnology2013
Enzymatic activity of a subtilisin homolog, Tk-SP, from Thermococcus kodakarensis in detergents and its ability to degrade the abnormal prion protein.
Article in BMC biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Combined computational, rational, and empirical design of boiling-resistant keratinase.Applied and environmental microbiology · 2026Article
- Propeptide-mediated enhancement of hyperthermophilic subtilisin-like protease expression in Escherichia coli.AMB Express · 2025Article
- Metal Nanomaterials and Hydrolytic Enzyme-Based Formulations for Improved Antifungal Activity.International journal of molecular sciences · 2023Review
- Identification, overexpression, purification, and biochemical characterization of a novel hyperthermostable keratinase from3 Biotech · 2021Article
- Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest.BMC biotechnology · 2019Article
- Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology.Biotechnology research international · 2016Article
- Article
- A Zinc-Dependent Protease AMZ-tk from a Thermophilic Archaeon is a New Member of the Archaemetzincin Protein Family.Frontiers in microbiology · 2015Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTk-SP is a member of subtilisin-like serine proteases from a hyperthermophilic archaeon Thermococcus kodakarensis. It has been known that the hyper-stable protease, Tk-SP, could exhibit enzymatic activity even at high temperature and in the presence of chemical denaturants. In this work, the enzymatic activity of Tk-SP was measured in the presence of detergents and EDTA. In addition, we focused to demonstrate that Tk-SP could degrade the abnormal prion protein (PrPSc), a protease-resistant isoform of normal prion protein (PrPC).
resultsTk-SP was observed to maintain its proteolytic activity with nonionic surfactants and EDTA at 80°C. We optimized the condition in which Tk-SP functions efficiently, and demonstrated that the enzyme is highly stable in the presence of 0.05% (w/v) nonionic surfactants and 0.01% (w/v) EDTA, retaining up to 80% of its activity. Additionally, we also found that Tk-SP can degrade PrPSc to a level undetectable by western-blot analysis.
conclusionsOur results indicate that Tk-SP has a great potential for technological applications, such as thermo-stable detergent additives. In addition, it is also suggested that Tk-SP-containing detergents can be developed to decrease the secondary infection risks of transmissible spongiform encephalopathies (TSE).
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