Versatility of subtilisin: a review on structure, characteristics, and applications
Due to its thermostability and high pH compatibility, subtilisin is most known for its role as an additive for detergents in which it is categorized as a serine protease according to MEROPS database. Subtilisin is typically isolated from various bacterial species of the Bacillus genus such as Bacill...
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| Format: | Article |
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John Wiley & Sons, Inc.
2022
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| Online Access: | http://psasir.upm.edu.my/id/eprint/102589/ |
| _version_ | 1848863837105684480 |
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| author | Mohd Azrin, Nur Aliyah Mohamad Ali, Mohd Shukuri Raja Abd Rahman, Raja Noor Zaliha Oslan, Siti Nurbaya Muhd Noor, Noor Dina |
| author_facet | Mohd Azrin, Nur Aliyah Mohamad Ali, Mohd Shukuri Raja Abd Rahman, Raja Noor Zaliha Oslan, Siti Nurbaya Muhd Noor, Noor Dina |
| author_sort | Mohd Azrin, Nur Aliyah |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Due to its thermostability and high pH compatibility, subtilisin is most known for its role as an additive for detergents in which it is categorized as a serine protease according to MEROPS database. Subtilisin is typically isolated from various bacterial species of the Bacillus genus such as Bacillus subtilis, B. amyloliquefaciens, B. licheniformis, and various other organisms. It is composed of 268–275 amino acid residues and is initially secreted in the precursor form, preprosubtilisin, which is composed of 29-residues signal peptide, 77-residues propeptide, and 275-residues active subtilisin. Subtilisin is known for the presence of high and low affinity calcium binding sites in its structure. Native subtilisin has general properties of thermostability, tolerance to neutral to high pH, broad specificity, and calcium-dependent stability, which contribute to the versatility of subtilisin applicability. Through protein engineering and immobilization technologies, many variants of subtilisin have been generated, which increase the applicability of subtilisin in various industries including detergent, food processing and packaging, synthesis of inhibitory peptides, therapeutic, and waste management applications. |
| first_indexed | 2025-11-15T13:39:15Z |
| format | Article |
| id | upm-102589 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T13:39:15Z |
| publishDate | 2022 |
| publisher | John Wiley & Sons, Inc. |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1025892024-03-12T04:18:34Z http://psasir.upm.edu.my/id/eprint/102589/ Versatility of subtilisin: a review on structure, characteristics, and applications Mohd Azrin, Nur Aliyah Mohamad Ali, Mohd Shukuri Raja Abd Rahman, Raja Noor Zaliha Oslan, Siti Nurbaya Muhd Noor, Noor Dina Due to its thermostability and high pH compatibility, subtilisin is most known for its role as an additive for detergents in which it is categorized as a serine protease according to MEROPS database. Subtilisin is typically isolated from various bacterial species of the Bacillus genus such as Bacillus subtilis, B. amyloliquefaciens, B. licheniformis, and various other organisms. It is composed of 268–275 amino acid residues and is initially secreted in the precursor form, preprosubtilisin, which is composed of 29-residues signal peptide, 77-residues propeptide, and 275-residues active subtilisin. Subtilisin is known for the presence of high and low affinity calcium binding sites in its structure. Native subtilisin has general properties of thermostability, tolerance to neutral to high pH, broad specificity, and calcium-dependent stability, which contribute to the versatility of subtilisin applicability. Through protein engineering and immobilization technologies, many variants of subtilisin have been generated, which increase the applicability of subtilisin in various industries including detergent, food processing and packaging, synthesis of inhibitory peptides, therapeutic, and waste management applications. John Wiley & Sons, Inc. 2022-12 Article PeerReviewed Mohd Azrin, Nur Aliyah and Mohamad Ali, Mohd Shukuri and Raja Abd Rahman, Raja Noor Zaliha and Oslan, Siti Nurbaya and Muhd Noor, Noor Dina (2022) Versatility of subtilisin: a review on structure, characteristics, and applications. Biotechnology and Applied Biochemistry, 69 (6). pp. 2599-2616. ISSN 0885-4513; ESSN: 1470-8744 https://iubmb.onlinelibrary.wiley.com/doi/10.1002/bab.2309 10.1002/bab.2309 |
| spellingShingle | Mohd Azrin, Nur Aliyah Mohamad Ali, Mohd Shukuri Raja Abd Rahman, Raja Noor Zaliha Oslan, Siti Nurbaya Muhd Noor, Noor Dina Versatility of subtilisin: a review on structure, characteristics, and applications |
| title | Versatility of subtilisin: a review on structure, characteristics, and applications |
| title_full | Versatility of subtilisin: a review on structure, characteristics, and applications |
| title_fullStr | Versatility of subtilisin: a review on structure, characteristics, and applications |
| title_full_unstemmed | Versatility of subtilisin: a review on structure, characteristics, and applications |
| title_short | Versatility of subtilisin: a review on structure, characteristics, and applications |
| title_sort | versatility of subtilisin: a review on structure, characteristics, and applications |
| url | http://psasir.upm.edu.my/id/eprint/102589/ http://psasir.upm.edu.my/id/eprint/102589/ http://psasir.upm.edu.my/id/eprint/102589/ |