Chemistry Department, Faculty of Sciences and Mathematics, Diponegoro University, Jl. Prof. Soedarto, SH., Tembalang, Semarang, Indonesia
BibTex Citation Data :
@article{JKSA64593, author = {Annisa Dila Febriyanti and Mukhammad Asy'ari}, title = {Characterization of a Halostable Metalloprotease from the Halophilic Bacterium Bacillus clausii J1G-0%B}, journal = {Jurnal Kimia Sains dan Aplikasi}, volume = {27}, number = {8}, year = {2024}, keywords = {Halophilic bacteria; Bacillus clausii; halostable protease; high salinity; Madura salt ponds}, abstract = { Protein plays a crucial role as a biocatalyst in various industries, particularly in breaking down proteins into amino acids. The demand for proteases capable of functioning under extreme conditions, such as high salinity, temperature, and pH, is increasing. To address this, the exploration of bacteria that produce stable proteases in such environments is essential. Bacillus clausii J1G-0%B, a halophilic bacterium isolated from Madura salt ponds, thrives in salinity levels of 0-20% NaCl. This study aims to obtain and characterize the protease produced by Bacillus clausii J1G-0%B, focusing on its activity and stability under extreme conditions. The research involved screening, production, and purification of the protease using ammonium sulfate fractionation and dialysis. Protease activity was measured using the Kunitz method, and protein content was determined using the Lowry method. Characterization included optimizing enzymatic conditions (pH, temperature, NaCl concentration), identifying metalloprotease types, and analyzing enzyme kinetics and thermodynamics. The study successfully produced protease using a halophilic medium with casein and 5% NaCl. After 96 hours of incubation, the protease exhibited a specific activity of 654.737 U/mg. Optimal activity was observed at pH 7, 50°C, and 10% NaCl, with stability between 2.5% and 15% NaCl concentration. Enzyme kinetics revealed a high affinity for casein, with a K M value of 0.164 mg/mL and V max of 13.182 µmol/mL·min. Thermodynamic analysis indicated high stability, as shown by a positive ΔG i value (+105.84 kJ/mol), a low inactivation constant (k i = 0.0031 min -1 ), and a long half-life (t ½ = 223.548 minutes). EDTA chelation tests confirmed that the protease is a metalloprotease. The halostable protease from Bacillus clausii J1G-0%B shows significant potential for industrial applications and bioremediation in high-salinity environments. }, issn = {2597-9914}, pages = {395--402} doi = {10.14710/jksa.27.8.395-402}, url = {https://ejournal.undip.ac.id/index.php/ksa/article/view/64593} }
Refworks Citation Data :
Protein plays a crucial role as a biocatalyst in various industries, particularly in breaking down proteins into amino acids. The demand for proteases capable of functioning under extreme conditions, such as high salinity, temperature, and pH, is increasing. To address this, the exploration of bacteria that produce stable proteases in such environments is essential. Bacillus clausii J1G-0%B, a halophilic bacterium isolated from Madura salt ponds, thrives in salinity levels of 0-20% NaCl. This study aims to obtain and characterize the protease produced by Bacillus clausii J1G-0%B, focusing on its activity and stability under extreme conditions. The research involved screening, production, and purification of the protease using ammonium sulfate fractionation and dialysis. Protease activity was measured using the Kunitz method, and protein content was determined using the Lowry method. Characterization included optimizing enzymatic conditions (pH, temperature, NaCl concentration), identifying metalloprotease types, and analyzing enzyme kinetics and thermodynamics. The study successfully produced protease using a halophilic medium with casein and 5% NaCl. After 96 hours of incubation, the protease exhibited a specific activity of 654.737 U/mg. Optimal activity was observed at pH 7, 50°C, and 10% NaCl, with stability between 2.5% and 15% NaCl concentration. Enzyme kinetics revealed a high affinity for casein, with a KM value of 0.164 mg/mL and Vmax of 13.182 µmol/mL·min. Thermodynamic analysis indicated high stability, as shown by a positive ΔGi value (+105.84 kJ/mol), a low inactivation constant (ki = 0.0031 min-1), and a long half-life (t½ = 223.548 minutes). EDTA chelation tests confirmed that the protease is a metalloprotease. The halostable protease from Bacillus clausii J1G-0%B shows significant potential for industrial applications and bioremediation in high-salinity environments.
Article Metrics:
Last update:
Last update: 2024-11-20 12:52:14
As an article writer, the author has the right to use their articles for various purposes, including use by institutions that employ authors or institutions that provide funding for research. Author rights are granted without special permission.
Author who publishes a paper at JKSA has the broad right to use their work for teaching and scientific purposes without the need to ask permission, including: used for (i) teaching in the author's class or institution, (ii) presentation at meetings or conferences and distributing copies to participants ; (iii) training conducted by the author or author's institution; (iv) distribution to colleagues for research use; (v) use in the compilation of subsequent authors' works; (vi) inclusion in a thesis or dissertation; (vi) reuse of part of the article in another work (with citation); (vii) preparation of derivative works (with citation); (viii) voluntary posting on open websites operated by authors or author institutions for scientific purposes (follow the CC BY-SA License).
Authors and readers can copy and redistribute material in any media or format, and mix, modify, and build material for any purpose but they must provide appropriate credit (provide article citation or content), providing links to the license, and indicate if there are changes.
The authors submitting a manuscript do so on the understanding that if accepted for publication, copyright of the article shall be assigned to Jurnal Kimia Sains dan Aplikasi (JKSA). Copyright encompasses rights to reproduce and deliver the article in all form and media, including reprints, photographs, microfilms and any other similar reproductions, as well as translations.
Reproduce any part of this journal, its storage in the database or its transmission by all forms or media is permitted does not need for written permission from JKSA. However, it should be cited as an honor in academic manners
JKSA and the Chemistry Department of Diponegoro University and the Editor make every effort to ensure that there are no data, opinions, or false or misleading statements published in JKSA. However, the content of the article is the sole and exclusive responsibility of each author.
The Copyright Transfer Form can be downloaded here: [Copyright Transfer Form - Indonesian] [Copyright Transfer Form - English]. The copyright form should be signed originally and send to the Editor in the form of printed letters, scanned documents sent via email or fax.
Adi Darmawan, Ph.D (Editor in Chief)
Editor in chief of Jurnal Kimia Sains dan Aplikasi (JKSA)
Chemistry Department, Faculty of Sciences and Mathematics, Diponegoro University
Visitor: View My Stats
Jurnal Kimia Sains dan Aplikasi is indexed in:
This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.