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An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: enzyme purification and characterization


Citation

Raja Abdul Rahman, Raja Noor Zaliha and Lee, Poh Geok and Basri, Mahiran and Salleh, Abu Bakar (2006) An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: enzyme purification and characterization. Enzyme and Microbial Technology, 39 (7). pp. 1484-1491. ISSN 0141-0229; ESSN: 1879-0909

Abstract / Synopsis

The organic solvent-tolerant strain K protease was purified to homogeneity by ammonium sulphate precipitation and anion exchange chromatography with 124-fold increase in specific activity. The molecular mass of the purified enzyme as revealed by SDS-PAGE electrophoresis is 51,000 Da. The strain K protease was an alkaline metalloprotease with an optimum pH and temperature of 10 and 70 °C, respectively. The enzyme showed stability and activation in the presence of organic solvents with log Pa/w values equal or more than 4.0. After 14 days of incubation, the purified protease was activated 1.11, 1.82, 1.50, 1.75 and 1.80 times in 1-decanol, isooctane, decane, dodecane and hexadecane, respectively.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
DOI Number: 10.1016/j.enzmictec.2006.03.038
Publisher: Elsevier
Keywords: Pseudomonas; Organic solvent-tolerant bacterium; Characterization; Organic solvent-stable enzyme; Alkaline metaloprotease
Depositing User: Erni Suraya Abdul Aziz
Date Deposited: 14 Jun 2010 09:27
Last Modified: 26 Sep 2016 16:53
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1016/j.enzmictec.2006.03.038
URI: http://psasir.upm.edu.my/id/eprint/7245
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