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
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.
Download File
Official URL or Download Paper: http://www.sciencedirect.com/science/article/pii/S...
|
Additional Metadata
Item Type: | Article |
---|---|
Divisions: | Faculty of Biotechnology and Biomolecular Sciences |
DOI Number: | https://doi.org/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 01:27 |
Last Modified: | 26 Sep 2016 08:53 |
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 |
Statistic Details: | View Download Statistic |
Actions (login required)
View Item |