ArticleApplied biochemistry and biotechnology2020
Preparation and Irreversible Inhibition Mechanism Insight into a Recombinant Kunitz Trypsin Inhibitor from Glycine max L. Seeds.
Article in Applied biochemistry and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Trypsinogen Pro-Region as a Molecular Scaffold for the Design of Competitive Peptide Inhibitors of Trypsin-Like Proteases.Archives of insect biochemistry and physiology · 2026Article
- Gene Cloning, Expression, and Purification of Kunitz Trypsin Inhibitor from Glycine max Using Halo Tag.Molecular biotechnology · 2026Article
- Heterologous expression and physicochemical characteristics identification of Kunitz protease inhibitor in3 Biotech · 2022Article
- Urease andEvidence-based complementary and alternative medicine : eCAM · 2022Article
- Structure-Activity Relationship and Molecular Docking of a Kunitz-Like Trypsin Inhibitor, Kunitzin-AH, from the Skin Secretion ofPharmaceutics · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soybean Kunitz trypsin inhibitor (SKTI), extracted from soybean (Glycine max L.) seeds, possesses insect resistance and anti-tumor properties. But its specific mechanisms of action are not yet known. This article reports an efficient method to produce recombinant SKTI (rSKTI) in Escherichia coli, reveals some biochemical properties of rSKTI, and discusses the inhibition mechanism of SKTI. The rSKTI was expressed as inclusion body in E. coli BL21 (DE3). After refolding, the active rSKTI was obtained and was further purified with anion-exchange chromatography (DEAE-FF) efficiently. There were similar biochemical properties between SKTI and rSKTI. The optimum pH and the optimum temperature were pH 8.0 and 35 °C, respectively, being stable during pH 7.0-11.0 and below 37 °C. The activity against trypsin was inhibited by Co
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