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:	Q179.9-180 Research
Online Access:	http://eprints.usm.my/42518/1/pBIO36.pdf http://eprints.usm.my/42518/
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Institution:	Universiti Sains Malaysia
Language:	English

id	my.usm.eprints.42518
record_format	eprints
spelling	my.usm.eprints.42518 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.
institution	Universiti Sains Malaysia
building	Hamzah Sendut Library
collection	Institutional Repository
continent	Asia
country	Malaysia
content_provider	Universiti Sains Malaysia
content_source	USM Institutional Repository
url_provider	http://eprints.usm.my/
language	English
topic	Q179.9-180 Research
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
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).
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
format	Book Section
author	Ibrahim, Noor Azlina Rahman, Raja Noor Zaliha R. Abd. Rahman, Mohd. Basyaruddin Abd. Basri, Mahiran Salleh, Abu Bakar
author_sort	Ibrahim, Noor Azlina
title	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_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_sort	structural conformation of bacillus stearothermophilus f1 protease and effect of modification on its thermostability
publisher	Penerbit Universiti Sains Malaysia
publishDate	2004
url	http://eprints.usm.my/42518/1/pBIO36.pdf http://eprints.usm.my/42518/
_version_	1643710517844377600

Structural conformation of Bacillus stearothermophilus F1 protease and effect of modification on its thermostability

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