Improved antimicrobial spectrum of the N-acetylmuramoyl-l-alanine amidase from Latilactobacillus sakei upon LysM domain deletion
Author:
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Physiology,Biotechnology
Link
https://link.springer.com/content/pdf/10.1007/s11274-021-03169-1.pdf
Reference43 articles.
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2. Akcapinar GB, Kappel L, Sezerman OU, Seidl-Seiboth V (2015) Molecular diversity of LysM carbohydrate-binding motifs in fungi. Curr Genet 61:103–113. https://doi.org/10.1007/s00294-014-0471-9
3. Anba-Mondoloni J, Chaillou S, Zagorec M, Champomier-Verges M (2013) Catabolism of N-acetylneuraminic acid, a fitness function of the food-borne lactic acid bacterium Lactobacillus sakei, involves two newly characterized proteins. Appl Environ Microbiol 79:2012–2018. https://doi.org/10.1128/AEM.03301-12
4. Buist G, Steen A, Kok J, Kuipers OP (2008) LysM, a widely distributed protein motif for binding to (peptido) glycans. Mol Microbiol 68:838–847. https://doi.org/10.1111/j.1365-2958.2008.06211.x
5. Chang Y (2020) Bacteriophage-derived endolysins applied as potent biocontrol agents to enhance food safety. Microorganisms 8(5):724. https://doi.org/10.3390/microorganisms8050724
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