ArticleBiomolecules2020
Improved Production and Biophysical Analysis of Recombinant Silicatein-α.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Product distribution in the silicatein-catalysed synthesis of polydimethylsiloxane.Catalysis science & technology · 2026Article
- Enhanced stability and reusability of recombinant silicatein upon biomimetic metal-organic framework crystallization.Chemical science · 2026Article
- Directed Evolution of Silicatein Reveals Biomineralization Synergism between Protein Sequences.ACS omega · 2025Article
- Understanding Biomineralization Mechanisms to Produce Size-Controlled, Tailored Nanocrystals for Optoelectronic and Catalytic Applications: A Review.ACS applied nano materials · 2024Review
- Evaluation of Fluorescence-Based Screening Assays for the Detection and Quantification of Silyl Hydrolase Activity.ACS omega · 2024Article
- Development of Improved Spectrophotometric Assays for Biocatalytic Silyl Ether Hydrolysis.Biomolecules · 2024Article
- Inorganic Polymeric Materials for Injured Tissue Repair: Biocatalytic Formation and Exploitation.Biomedicines · 2022Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Silicatein-α is a hydrolase found in siliceous sea sponges with a unique ability to condense and hydrolyse silicon-oxygen bonds. The enzyme is thus of interest from the perspective of its unusual enzymology, and for potential applications in the sustainable synthesis of siloxane-containing compounds. However, research into this enzyme has previously been hindered by the tendency of silicatein-α towards aggregation and insolubility. Herein, we report the development of an improved method for the production of a trigger factor-silicatein fusion protein by switching the previous hexahistidine tag for a Strep-II tag, resulting in 244-fold improvement in protein yield compared to previous methods. Light scattering and thermal denaturation analyses show that under the best storage conditions, although oligomerisation is never entirely abolished, these nanoscale aggregates of the Strep-tagged protein exhibit improved colloidal stability and solubility. Enzymatic assays show that the Strep-tagged protein retains catalytic competency, but exhibits lower activity compared to the His
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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.