Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2
Abstract Background L-arginase, is a powerful anticancer that hydrolyzes L-arginine to L-ornithine and urea. This enzyme is widely distributed and expressed in organisms like plants, fungi, however very scarce from bacteria. Our study is based on isolating, purifying, and screening the marine bacter...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2024-01-01
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| Series: | BMC Biotechnology |
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| Online Access: | https://doi.org/10.1186/s12896-024-00829-6 |
| _version_ | 1797276455854407680 |
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| author | Manal S. Selim Marwa M. Mounier Sayeda A. Abdelhamid Ahmed Abdelghani Hamed Mostafa M. Abo Elsoud Sahar S. Mohamed |
| author_facet | Manal S. Selim Marwa M. Mounier Sayeda A. Abdelhamid Ahmed Abdelghani Hamed Mostafa M. Abo Elsoud Sahar S. Mohamed |
| author_sort | Manal S. Selim |
| collection | DOAJ |
| description | Abstract Background L-arginase, is a powerful anticancer that hydrolyzes L-arginine to L-ornithine and urea. This enzyme is widely distributed and expressed in organisms like plants, fungi, however very scarce from bacteria. Our study is based on isolating, purifying, and screening the marine bacteria that can produce arginase. Results The highest arginase producing bacteria will be identified by using microbiological and molecular biology methods as Bacillus licheniformis OF2. Characterization of arginase is the objective of this study. The activity of enzyme was screened, and estimated beside partial sequencing of arginase gene was analyzed. In silico homology modeling was applied to generate the protein's 3D structure, and COACH and COFACTOR were applied to determine the protein's binding sites and biological annotations based on the I-TASSER structure prediction. The purified enzyme was undergone an in vitro anticancer test. Conclusions L-arginase demonstrated more strong anti-cancer cells with an IC50 of 21.4 ug/ml in a dose-dependent manner. L-arginase underwent another investigation for its impact on the caspase 7 and BCL2 family of proteins (BCL2, Bax, and Bax/Bcl2). Through cell arrest in the G1/S phase, L-arginase signals the apoptotic cascade, which is supported by a flow cytometry analysis of cell cycle phases. |
| first_indexed | 2024-03-07T15:28:29Z |
| format | Article |
| id | doaj.art-2a028875e73b4518b47130ea88d20c74 |
| institution | Directory Open Access Journal |
| issn | 1472-6750 |
| language | English |
| last_indexed | 2024-03-07T15:28:29Z |
| publishDate | 2024-01-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Biotechnology |
| spelling | doaj.art-2a028875e73b4518b47130ea88d20c742024-03-05T16:33:52ZengBMCBMC Biotechnology1472-67502024-01-0124111610.1186/s12896-024-00829-6Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2Manal S. Selim0Marwa M. Mounier1Sayeda A. Abdelhamid2Ahmed Abdelghani Hamed3Mostafa M. Abo Elsoud4Sahar S. Mohamed5Microbial Biotechnology Department, National Research CentrePharmacognosy Department, National Research CentreMicrobial Biotechnology Department, National Research CentreMicrobial Chemistry Department, National Research CentreMicrobial Biotechnology Department, National Research CentreMicrobial Biotechnology Department, National Research CentreAbstract Background L-arginase, is a powerful anticancer that hydrolyzes L-arginine to L-ornithine and urea. This enzyme is widely distributed and expressed in organisms like plants, fungi, however very scarce from bacteria. Our study is based on isolating, purifying, and screening the marine bacteria that can produce arginase. Results The highest arginase producing bacteria will be identified by using microbiological and molecular biology methods as Bacillus licheniformis OF2. Characterization of arginase is the objective of this study. The activity of enzyme was screened, and estimated beside partial sequencing of arginase gene was analyzed. In silico homology modeling was applied to generate the protein's 3D structure, and COACH and COFACTOR were applied to determine the protein's binding sites and biological annotations based on the I-TASSER structure prediction. The purified enzyme was undergone an in vitro anticancer test. Conclusions L-arginase demonstrated more strong anti-cancer cells with an IC50 of 21.4 ug/ml in a dose-dependent manner. L-arginase underwent another investigation for its impact on the caspase 7 and BCL2 family of proteins (BCL2, Bax, and Bax/Bcl2). Through cell arrest in the G1/S phase, L-arginase signals the apoptotic cascade, which is supported by a flow cytometry analysis of cell cycle phases.https://doi.org/10.1186/s12896-024-00829-6ArginaseBacillus licheniformis OF2Silico homologyAnti-cancer |
| spellingShingle | Manal S. Selim Marwa M. Mounier Sayeda A. Abdelhamid Ahmed Abdelghani Hamed Mostafa M. Abo Elsoud Sahar S. Mohamed Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2 BMC Biotechnology Arginase Bacillus licheniformis OF2 Silico homology Anti-cancer |
| title | Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2 |
| title_full | Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2 |
| title_fullStr | Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2 |
| title_full_unstemmed | Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2 |
| title_short | Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2 |
| title_sort | characterization modeling and anticancer activity of l arginase production from marine bacillus licheniformis of2 |
| topic | Arginase Bacillus licheniformis OF2 Silico homology Anti-cancer |
| url | https://doi.org/10.1186/s12896-024-00829-6 |
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