Heterologous expression and physicochemical characteristics identification of Kunitz protease inhibitor in Brassica napus
Author:
Publisher
Springer Science and Business Media LLC
Subject
Agricultural and Biological Sciences (miscellaneous),Environmental Science (miscellaneous),Biotechnology
Link
https://link.springer.com/content/pdf/10.1007/s13205-022-03149-8.pdf
Reference31 articles.
1. Bei Z, Zhang H, Lei W et al (2018) Characterization of 16-kDa major allergen with α-amylase inhibitor domain in Tartary buckwheat seeds. Mol Immunol 94:121–130. https://doi.org/10.1016/j.molimm.2017.12.024
2. Bendre A, Ramasamy S, Suresh CG (2018) Analysis of Kunitz inhibitors from plants for comprehensive structural and functional insights. Int J Biol Macromol 113:933–943. https://doi.org/10.1016/j.ijbiomac.2018.02.148
3. Cotabarren J, Lufrano D, Parisi MG et al (2020) Biotechnological, biomedical, and agronomical applications of plant protease inhibitors with high stability: a systematic review. Plant Sci 292:110398. https://doi.org/10.1016/j.plantsci.2019.110398
4. de Barros KMA, de Cássia Orlandi Sardi J, Maria-Neto S et al (2021) A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria. Biomed Pharmacother 144:112198. https://doi.org/10.1016/j.biopha.2021.112198
5. Dermawan D, Prabowo BA, Rakhmadina CA (2021) In silico study of medicinal plants with cyclodextrin inclusion complex as the potential inhibitors against SARS-CoV-2 main protease (Mpro) and spike (S) receptor. Inform Med Unlocked 25:100645. https://doi.org/10.1016/j.imu.2021.100645
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