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

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.

Preview

PDF Download (410kB) | Preview

Abstract

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).

Item Type:	Book Section
Subjects:	Q Science > Q Science (General) > Q179.9-180 Research
Divisions:	Koleksi Penganjuran Persidangan (Conference Collection) > Annual Seminar National Science Fellowship (NSF)
Depositing User:	Puan Sukmawati Muhamad
Date Deposited:	15 Oct 2018 08:04
Last Modified:	01 Nov 2018 01:23
URI:	http://eprints.usm.my/id/eprint/42518

Actions (login required)

View Item