detergent stability
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2015 ◽  
Vol 28 (6) ◽  
pp. 147-151 ◽  
Author(s):  
Selin Ece ◽  
Serap Evran ◽  
Jan-Oliver Janda ◽  
Rainer Merkl ◽  
Reinhard Sterner

2014 ◽  
Vol 1838 (11) ◽  
pp. 2817-2824 ◽  
Author(s):  
Daniel J. Scott ◽  
Lutz Kummer ◽  
Pascal Egloff ◽  
Ross A.D. Bathgate ◽  
Andreas Plückthun

2012 ◽  
Vol 422 (3) ◽  
pp. 414-428 ◽  
Author(s):  
Karola M. Schlinkmann ◽  
Matthias Hillenbrand ◽  
Alexander Rittner ◽  
Madeleine Künz ◽  
Ralf Strohner ◽  
...  

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.


Structure ◽  
2011 ◽  
Vol 19 (1) ◽  
pp. 17-25 ◽  
Author(s):  
Yo Sonoda ◽  
Simon Newstead ◽  
Nien-Jen Hu ◽  
Yilmaz Alguel ◽  
Emmanuel Nji ◽  
...  

1992 ◽  
Vol 99 (3) ◽  
pp. 830-836 ◽  
Author(s):  
Norman P. A. Huner ◽  
Douglas Campbell ◽  
Marianna Krol ◽  
Donald B. Hayden ◽  
Elizabeth M. Myscich ◽  
...  

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