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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Main Authors: Ibrahim, Noor Azlina, Rahman, Raja Noor Zaliha R. Abd., Rahman, Mohd. Basyaruddin Abd., Basri, Mahiran, Salleh, Abu Bakar
Other Authors: Ahmad, Abdul Latif
Format: Book Section
Language:English
Published: Penerbit Universiti Sains Malaysia 2004
Subjects:
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