Self-cleaved expression of recombinant lysostaphin from its cellulose binding domain fusion
Author:
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Biotechnology
Link
https://link.springer.com/content/pdf/10.1007/s00253-022-12047-1.pdf
Reference30 articles.
1. Bastos MCF, Coutinho BG, Coelho MLV (2010) Lysostaphin: a Staphylococcal bacteriolysin with potential clinical applications. Pharmaceuticals 3(4):1139–1161. https://doi.org/10.3390/ph3041139
2. Charlton A, Zachariou M (2011) Tag removal by site-specific cleavage of recombinant fusion proteins. Methods Mol Biol 681:349–367. https://doi.org/10.1007/978-1-60761-913-0_19
3. Chen KJ, Wu YT, Lee CK (2019) Cellulose binding domain fusion enhanced soluble expression of fructosyl peptide oxidase and its simultaneous purification and immobilization. Int J Biol Macromol 133:980–986. https://doi.org/10.1016/j.ijbiomac.2019.04.171
4. Costa S, Almeida A, Castro A, Domingues L (2014) Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system. Front Microbiol 5:63. https://doi.org/10.3389/fmicb.2014.00063
5. Dai G, Hu J, Zhao X, Wang P (2017) A colorimetric paper sensor for lactate assay using a cellulose-binding recombinant enzyme. Sens Actuators B Chem 238:138–144. https://doi.org/10.1016/j.snb.2016.07.008
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1. Peptidoglycan-Targeting Staphylolytic Enzyme Lysostaphin as a Novel and Efficient Protease toward Glycine-Rich Flexible Peptide Linkers;Journal of Agricultural and Food Chemistry;2023-03-27
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