Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability
The extracellular F1 serine protease, produced by a thermophilic Bacillus stearothermophilus F1, has been isolated and characterized as one of a serine protease. F1 protease was stable in the pH range of 8.0 to 10.0, with an optimum activity at pH 9.0. The enzyme was stable for 24h at 70°C (Rahman...
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| Format: | Book Section |
| Language: | English |
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Penerbit Universiti Sains Malaysia
2004
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| Online Access: | http://eprints.usm.my/42518/ http://eprints.usm.my/42518/1/pBIO36.pdf |
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| author | Ibrahim, Noor Azlina Rahman, Raja Noor Zaliha R. Abd. Rahman, Mohd. Basyaruddin Abd. Basri, Mahiran Salleh, Abu Bakar |
| author2 | Ahmad, Abdul Latif |
| author_facet | Ahmad, Abdul Latif Ibrahim, Noor Azlina Rahman, Raja Noor Zaliha R. Abd. Rahman, Mohd. Basyaruddin Abd. Basri, Mahiran Salleh, Abu Bakar |
| author_sort | Ibrahim, Noor Azlina |
| building | USM Institutional Repository |
| collection | Online Access |
| description | The extracellular F1 serine protease, produced by a thermophilic Bacillus stearothermophilus F1, has been isolated and characterized as one of a serine protease. F1
protease was stable in the pH range of 8.0 to 10.0, with an optimum activity at pH 9.0. The enzyme was stable for 24h at 70°C (Rahman et al., 1994). |
| first_indexed | 2025-11-15T17:49:31Z |
| format | Book Section |
| id | usm-42518 |
| institution | Universiti Sains Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T17:49:31Z |
| publishDate | 2004 |
| publisher | Penerbit Universiti Sains Malaysia |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | usm-425182018-11-01T01:23:55Z http://eprints.usm.my/42518/ Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability Ibrahim, Noor Azlina Rahman, Raja Noor Zaliha R. Abd. Rahman, Mohd. Basyaruddin Abd. Basri, Mahiran Salleh, Abu Bakar Q179.9-180 Research The extracellular F1 serine protease, produced by a thermophilic Bacillus stearothermophilus F1, has been isolated and characterized as one of a serine protease. F1 protease was stable in the pH range of 8.0 to 10.0, with an optimum activity at pH 9.0. The enzyme was stable for 24h at 70°C (Rahman et al., 1994). Penerbit Universiti Sains Malaysia Ahmad, Abdul Latif Yahya, Ahmad Rahim Mohd Abdullah, Amirul AI-Ashraf Muhammad, Tengku Sifzizul Tengku 2004 Book Section PeerReviewed application/pdf en http://eprints.usm.my/42518/1/pBIO36.pdf Ibrahim, Noor Azlina and Rahman, Raja Noor Zaliha R. Abd. and Rahman, Mohd. Basyaruddin Abd. and Basri, Mahiran and Salleh, Abu Bakar (2004) Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability. In: The 4th Annual Seminar of National Science Fellowship NSF 2004 Proceedings. Penerbit Universiti Sains Malaysia, Pulau Pinang, Malaysia, pp. 187-189. |
| spellingShingle | Q179.9-180 Research Ibrahim, Noor Azlina Rahman, Raja Noor Zaliha R. Abd. Rahman, Mohd. Basyaruddin Abd. Basri, Mahiran Salleh, Abu Bakar Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability |
| title | Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability |
| title_full | Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability |
| title_fullStr | Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability |
| title_full_unstemmed | Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability |
| title_short | Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability |
| title_sort | structural conformation of bacillus stearothermophilus f1 protease and effect of modification on its thermostability |
| topic | Q179.9-180 Research |
| url | http://eprints.usm.my/42518/ http://eprints.usm.my/42518/1/pBIO36.pdf |