Ji Min Lee
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Ji Min Lee has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
- Hasan Tarek
Department of Pharmacy, College of Pharmacy, Chosun University, Gwangju 61452, Republic of Korea
1 shared publication - Jin Cheol Yoo
Department of Pharmacy, College of Pharmacy, Chosun University, Gwangju 61452, Republic of Korea
1 shared publication - Kyung Bin Nam
Department of Pharmacy, College of Pharmacy, Chosun University, Gwangju 61452, Republic of Korea
1 shared publication - Sang Hun Lee
Department of Pharmacy, College of Pharmacy, Chosun University, Gwangju 61452, Republic of Korea
1 shared publication - Seung-Sik Cho
Department of Biomedicine, Health & Life Convergence Sciences, BK21 Four, Biomedical and Healthcare Research Institute, Mokpo National University, Muan-gun 58554, Jeonnam, Republic of Korea
1 shared publication
Latest Publications
- Open Access
- 27 June 2024
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 25 (13) , 7046
Mode of Action of Antimicrobial Potential Protease SH21 Derived from Bacillus siamensis
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.
- 27 June 2024
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 25 (13) , 7046
Open AccessMode of Action of Antimicrobial Potential Protease SH21 Derived from Bacillus siamensis
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.