Mode of Action of Antimicrobial Potential Protease SH21 Derived from Bacillus siamensis
Open Access
- 27 June 2024
- journal article
- research article
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 25 (13) , 7046
Abstract
Global public health is facing a major issue with emerging resistance to antimicrobial agents. Antimicrobial agents that are currently on the market are strong and efficient, but it has not been ruled out that these medications will eventually cause resistance to bacteria. Exploring novel bioactive compounds derived from natural sources is therefore, crucial to meet future demands. The present study evaluated the mode of action of the antimicrobial potential protease enzyme SH21. Protease SH21 exhibited antimicrobial activity, strong heat stability (up to 100 °C), and pH stability (pH 3.0 to 9.0). In terms of mode of action, we found that protease SH21 was able to disrupt the bacterial cell membrane as the results of the nucleotide leakage and cell membrane permeability assay. In addition, we also checked inner membrane permeability by PI uptake assay which suggested that protease SH21 has the ability to enter the bacterial cell membrane. Our results revealed that the antimicrobial protease SH21 might be a promising candidate for treating microbial infections.Keywords
Funding Information
- Chosun University (2023)
This publication has 16 references indexed in Scilit:
- Antibacterial and anti-biofilm activity, and mechanism of action of pleurocidin against drug resistant Staphylococcus aureusMicrobial Pathogenesis, 2019
- Antibacterial serine protease from Wrightia tinctoria: Purification and characterizationPlant Physiology and Biochemistry, 2017
- Antibacterial Activity of Extracellular Protease Isolated From an Algicolous Fungus Xylaria psidii KT30 Against Gram-Positive BacteriaHAYATI Journal of Biosciences, 2016
- Membrane disruption and DNA binding of Staphylococcus aureus cell induced by a novel antimicrobial peptide produced by Lactobacillus paracasei subsp. tolerans FX-6Food Control, 2016
- Efficient Screening of a Novel Antimicrobial Peptide from Jatropha curcas by Cell Membrane Affinity ChromatographyJournal of Agricultural and Food Chemistry, 2011
- Identification and Characterization of an Antibacterial Peptide of the 26-kDa Protease of Sarcophaga peregrina with Antibacterial ActivityThe Journal of Biochemistry, 2001
- Whole genome sequencing of meticillin-resistant Staphylococcus aureusThe Lancet, 2001
- Purification and Characterization of an Extracellular Protease from the Fish Pathogen Yersinia ruckeri and Effect of Culture Conditions on ProductionApplied and Environmental Microbiology, 1999
- The Novel Antibacterial Peptide Ceratotoxin A Alters Permeability of the Inner and Outer Membrane of Escherichia coli K-12Current Microbiology, 1996
- The Induced (Adaptive) Biosynthesis of -Galactosidase in Staphylococcus aureusJournal of General Microbiology, 1955