Isolation and characterization of alkalophilic Pseudomonas sp. and optimization of culture conditions for alkaline protease production

2012 ◽  
Vol 3 (1) ◽  
pp. 405-409
Author(s):  
B. Sreedevi B. Sreedevi ◽  
◽  
A. Abhigna A. Abhigna ◽  
J. Pramoda Kumari J. Pramoda Kumari
2011 ◽  
Vol 10 (14) ◽  
pp. 2733-2740 ◽  
Author(s):  
Liu Jianguo ◽  
Zhang Zhiqiang ◽  
Zhu Hu ◽  
Dang Hongyue ◽  
Lu Jianren ◽  
...  

2006 ◽  
Vol 9 (11) ◽  
pp. 2122-2126 ◽  
Author(s):  
Sidra Aftab ◽  
Samia Ahmed . ◽  
Sadia Saeed . ◽  
Sheikh Ajaz Rasool .

2016 ◽  
Vol 75 (5) ◽  
Author(s):  
Abdullah M. El Mahdi ◽  
Hamidi Abdul Aziz ◽  
Salem S. Abu Amr ◽  
Nour Sh El-Gendy ◽  
Hussein N. Nassar

2012 ◽  
Vol 2012 ◽  
pp. 1-13 ◽  
Author(s):  
Biswanath Bhunia ◽  
Apurba Dey

The optimization of physiochemical parameters for alkaline protease production using Bacillus licheniformis NCIM 2042 were carried out by Plackett-Burman design and response surface methodology (RSM). The model was validated experimentally and the maximum protease production was found 315.28 U using optimum culture conditions. The protease was purified using ammonium sulphate (60%) precipitation technique. The HPLC analysis of dialyzed sample showed that the retention time is 1.84 min with 73.5% purity. This enzyme retained more than 92% of its initial activity after preincubation for 30 min at 37∘C in the presence of 25% v/v DMSO, methanol, ethanol, ACN, 2-propanol, benzene, toluene, and hexane. In addition, partially purified enzyme showed remarkable stability for 60 min at room temperature, in the presence of anionic detergent (Tween-80 and Triton X-100), surfactant (SDS), bleaching agent (sodium perborate and hydrogen peroxide), and anti-redeposition agents (Na2CMC, Na2CO3). Purified enzyme containing 10% w/v PEG 4000 showed better thermal, surfactant, and local detergent stability.


1989 ◽  
Vol 42 (10) ◽  
pp. 1460-1464 ◽  
Author(s):  
JUN''ICHI SHOJI ◽  
HIROSHI HINOO ◽  
TERUO HATTORI ◽  
KEIICHIRO HIROOKA ◽  
YASUO KIMURA ◽  
...  

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