scholarly journals Lipase from New Isolate Bacillus cereus ATA179: Optimization of Production Conditions, Partial Purification, Characterization and Its Potential in the Detergent Industry

2014 ◽  
Vol 11 (2) ◽  
pp. 1056-1061
Author(s):  
Baghdad Science Journal

Three strain of Bacillus cereus were obtained from soil sours Laboratories of Biology Department/ College of Science/ University of Baghdad. The bacteria secreted extracellular xylanase in liquid cultur the test ability of xylanase production from these isolates was studied semi quantitative and quantitative screening appeared that Bacillus cereus X3 was the highest xylanase producer. The enzyme was partial purification 191 fold from cultur by reached step by 4 U/mg proteins by ammonium sulfat precipitation 80%, Ion exchang DEAE-cellulos chromatography Characterization study of the partial purifation enzyme revealed that the enzyme had a optimum activity pH8 and activity was stable in the pH rang (8-10) for 30min. maximal activity was attained at 50C


2005 ◽  
Vol 127 (3) ◽  
pp. 143-156 ◽  
Author(s):  
Monika Prakash ◽  
Rathindra Mohan Banik ◽  
Claudia Koch-Brandt

2020 ◽  
Author(s):  
Samina Naz Mukry ◽  
Sumbul Nazar ◽  
Muhammad Sohail ◽  
Shakeel Ahmed Khan

Abstract Background: The microorganisms are preferred over plants and animals for the bulk production of industrially important enzymes like pectinases because of their low production-cost, availability of fermentation raw material and the easily controllable production conditions. The pectinolytic potential of a large pool (130) of Bacillus cereus group and non-Bacillus cereus was evaluated. The effect of different physicochemical parameters on polygalacturonase(PGase) production by three promising strains, B. pumilusS76, B.thuringiensis S140(b) and B.taquilensis S140(c) with gene bank accession no. KU981112, KU981113 and KU981114, were studied and the enzyme was partially characterized. The enzyme activity was assayed using dinitrosalicylic acid method.Results: The polygalacturonases produced by Bp S76, Bt S140(b) and BtqS140(c) were thermostable at temperature above 55ºC with a melting temperature (Tm) of 72ºC,62ºC and 57ºC, respectively and the half-life (T1/2) at 60ºC of 50, 65 and 30 min., respectively. The catabolite repression was noted in presence of glucose while the production increased upon addition of 1% yeast extract to the growth medium. The enzyme activity was also induced in presence of Na+ and Ca+2.Conclusion: The strain Bp S76 appeared a better candidate for future biotechnological application owing to the production of higher titers (6.11 IU/L.hrs) of polygalacturonase with greater stability.


2013 ◽  
Vol 115 (2) ◽  
pp. 358-366 ◽  
Author(s):  
I. Hammami ◽  
R. Siala ◽  
M. Jridi ◽  
N. Ktari ◽  
M. Nasri ◽  
...  

1994 ◽  
Vol 11 (2) ◽  
pp. 113-117
Author(s):  
Takahisa MIYAMOTO ◽  
Kazumi MIYAKO ◽  
Jun NAKAMURA ◽  
Shoji HATANO

2021 ◽  
Vol 43 ◽  
pp. e51486
Author(s):  
Cengiz Çorbacı ◽  
Kadriye Özcan

Microbial enzymes are used as organic catalysts in different industrial processes. In this study, we aimed to produce and investigate alkaline proteases from a novel actinobacterium strain isolated from a Black Sea marine sediment. The optimal production conditions for Streptomyces sp. K47 alkaline proteases was 4-days incubation at 28ºC in a salt-free medium buffered with 50 mM Tris-HCl buffer (pH 9.0) and containing glucose (1.0%, w v-1) and yeast extract (0.5%, w v-1). The enzyme solution was partially purified using (NH4)2SO4 precipitation (40-70%). After desalting, it was purified 1-84 fold with a recovery of 19.42%. Zymogram analyses revealed the presence of more than one protease enzyme. The enzyme solution exhibited maximum activity at pH 9.0 and 37ºC, remaining stable after a 2-hour incubation at all tested conditions. Streptomyces sp. K47 has the potential to be used in industrial processes because of its ability to produce multiple protease enzymes displaying stability in a broad pH and temperature range.


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