Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly
Proteases are abundantly found in all living organisms that are essential to life. Microbial proteases possess a commercial value with various applications in industries. Some of the biotechnological applications are involved detergents, leather, food, pharmaceutical and bioremediation processes. Th...
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| Format: | Article |
| Language: | English |
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Universiti Teknologi MARA, Negeri Sembilan
2017
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| Online Access: | https://ir.uitm.edu.my/id/eprint/29361/ |
| _version_ | 1848807214827962368 |
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| author | Sulaiman, Noorulaini Mahadi, Nor Muhammad Ramly, Nur Zazarina |
| author_facet | Sulaiman, Noorulaini Mahadi, Nor Muhammad Ramly, Nur Zazarina |
| author_sort | Sulaiman, Noorulaini |
| building | UiTM Institutional Repository |
| collection | Online Access |
| description | Proteases are abundantly found in all living organisms that are essential to life. Microbial proteases possess a commercial value with various applications in industries. Some of the biotechnological applications are involved detergents, leather, food, pharmaceutical and bioremediation processes. The aim of the study is to analyses the binding cavities in protease, BleG1_1979, from Bacillus lehensis G1, in order to examine the interaction site of protease with other molecules. Protein encoding for BleG1_1979 is 19.2 kDa in size, with a predicted pI value
of 5.35 and 42% identity with intracellular protease from Thermococcus onnurineus NA1 from PDB database. Molecular docking was run using Hex v8.0.0. Four substrates were docked to BleG1_1979 pocket cavities, and casein exhibited highest binding affinity as compared to
collagen, gelatin and keratin. This has suggested that BleG1_1979 could rapidly hydrolyzed casein and B. lehensis G1 did not contain keratolytic activity. Docking results have provided a basis for further understanding the molecular mechanism of substrates preference for B. lehensis G1 protease. Such knowledge could be explored to expand the usefulness of microbial protease for industrial application. |
| first_indexed | 2025-11-14T22:39:16Z |
| format | Article |
| id | uitm-29361 |
| institution | Universiti Teknologi MARA |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T22:39:16Z |
| publishDate | 2017 |
| publisher | Universiti Teknologi MARA, Negeri Sembilan |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | uitm-293612020-04-08T10:53:41Z https://ir.uitm.edu.my/id/eprint/29361/ Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly joa Sulaiman, Noorulaini Mahadi, Nor Muhammad Ramly, Nur Zazarina Polymers. Macromolecules Biochemistry Biotechnology Proteases are abundantly found in all living organisms that are essential to life. Microbial proteases possess a commercial value with various applications in industries. Some of the biotechnological applications are involved detergents, leather, food, pharmaceutical and bioremediation processes. The aim of the study is to analyses the binding cavities in protease, BleG1_1979, from Bacillus lehensis G1, in order to examine the interaction site of protease with other molecules. Protein encoding for BleG1_1979 is 19.2 kDa in size, with a predicted pI value of 5.35 and 42% identity with intracellular protease from Thermococcus onnurineus NA1 from PDB database. Molecular docking was run using Hex v8.0.0. Four substrates were docked to BleG1_1979 pocket cavities, and casein exhibited highest binding affinity as compared to collagen, gelatin and keratin. This has suggested that BleG1_1979 could rapidly hydrolyzed casein and B. lehensis G1 did not contain keratolytic activity. Docking results have provided a basis for further understanding the molecular mechanism of substrates preference for B. lehensis G1 protease. Such knowledge could be explored to expand the usefulness of microbial protease for industrial application. Universiti Teknologi MARA, Negeri Sembilan 2017 Article PeerReviewed text en https://ir.uitm.edu.my/id/eprint/29361/1/29361.pdf Sulaiman, Noorulaini and Mahadi, Nor Muhammad and Ramly, Nur Zazarina (2017) Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly. (2017) Journal of Academia <https://ir.uitm.edu.my/view/publication/Journal_of_Academia.html>, 5 (1). pp. 36-43. ISSN 2289-6368 https://nsembilan.uitm.edu.my/joacns/ |
| spellingShingle | Polymers. Macromolecules Biochemistry Biotechnology Sulaiman, Noorulaini Mahadi, Nor Muhammad Ramly, Nur Zazarina Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly |
| title | Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly |
| title_full | Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly |
| title_fullStr | Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly |
| title_full_unstemmed | Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly |
| title_short | Substrate binding site of proteases from bacillus lehensis G1 by molecular docking / Noorulaini Sulaiman, Nor Muhammad Mahadi and Nur Zazarina Ramly |
| title_sort | substrate binding site of proteases from bacillus lehensis g1 by molecular docking / noorulaini sulaiman, nor muhammad mahadi and nur zazarina ramly |
| topic | Polymers. Macromolecules Biochemistry Biotechnology |
| url | https://ir.uitm.edu.my/id/eprint/29361/ https://ir.uitm.edu.my/id/eprint/29361/ |