scholarly journals Ultrasound assisted process intensification of uricase and alkaline protease enzyme co-production in Bacillus licheniformis

2018 ◽  
Vol 45 ◽  
pp. 173-179 ◽  
Author(s):  
Shweta V. Pawar ◽  
Virendra K. Rathod
Keyword(s):  
Bacillus Licheniformis ◽  
Alkaline Protease ◽  
Process Intensification ◽  
Protease Enzyme ◽  
Ultrasound Assisted

scholarly journals Purification, characterization and application of novel alkaline protease from new Bacillus cereus UV-15 mutant

2017 ◽  
Vol 7 (4) ◽  
pp. 1 ◽  
Author(s):  
Sreedevi Basavaraju ◽  
Chandrasekhar Kathera ◽  
Pramoda Kumari Jasti
Keyword(s):  
Bacillus Cereus ◽  
Ammonium Sulphate ◽  
Alkaline Protease ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Industrial Applications ◽  
Tween 20 ◽  
Original Activity ◽  
Protease Enzyme

The alkaline protease produced by Bacillus cereus UV-15 mutant was purified by precipitation with ammonium sulphate and gel filtration through sephadex G-100. The enzyme has shown to have a molecular weight of 29kDa by SDS polyacrylamide gel electrophoresis. The extracted protease enzyme was purified by 16.64 fold through ammonium sulphate precipitation and chromatography separation in Sephadex G-100. The purified protease had a specific activity of 2915 (U/mg). The zymogram also revealed a clear hydrolytic zone due to proteolytic activity, which coincided with the band obtained with SDS–PAGE. The enzyme was remained active and stable at pH 8-11, with an optimum at pH 10.0. The protease was stable in the temperature ranging from 40°C to 60°C, but gradually decreased at temperature 70°C. The optimum temperature for protease activity was determined at 60°C. The enzyme showed stability towards non-ionic and anionic surfactants, and oxidizing agents. At 1% concentration of Tween-20 and Tween-80, the enzyme retained 78% and 94% relative activity respectively. Alkaline protease retained 95% activity toward 0.5% concentration of the anionic detergent SDS. The enzyme showed compatibility at 50°C with commercial detergents such as Ariel, Surf excel, Rin, wheel, Tide and Nirma. In the presence of Ariel and Rin the enzyme retained about 72 and 75% of the original activity respectively. The supplementation of the enzyme in detergents could improve the cleansing performance towards the blood stains and suggested to be used as a detergent additive. The enzyme also removed goat hide hairs completely after 15 hr of incubation. These characteristics may make the enzyme suitable for several industrial applications, especially in leather industries.

scholarly journals Gelatin production using fish wastes by extracted alkaline protease from Bacillus licheniformis

2018 ◽  
Vol 55 (12) ◽  
pp. 5175-5180 ◽  
Author(s):  
Armin Mirzapour Kouhdasht ◽  
Marzieh Moosavi-Nasab ◽  
Mahmood Aminlari
Keyword(s):  
Bacillus Licheniformis ◽  
Alkaline Protease

scholarly journals Characterization of an alkaline protease with high quality bating potential in leather processing from Bacillus licheniformis MZK05M9 mutant

2015 ◽  
Vol 3 (1) ◽  
pp. 36 ◽  
Author(s):  
Md. Arafat Al Mamun ◽  
Md. Murad Khan ◽  
Md. Nahinur Rahmam Akand ◽  
Shakila Nargis Khan ◽  
Md. Mozammel Hoq
Keyword(s):  
Bacillus Licheniformis ◽  
Alkaline Protease ◽  
Specific Activity ◽  
Water Vapor Permeability ◽  
Vapor Permeability ◽  
Ph Optimum ◽  
Crude Enzyme Extract ◽  
Leather Processing ◽  
Stain Removal ◽  
The Stability

<p>An alkaline protease from <em>Bacillus licheniformis</em> MZK05M9 (<em>Bl</em>M9), a mutant strain developed in our laboratory, has been partially purified and characterized for its robustness and eco-friendly application potential in processing of hides and skins for leather manufacturing and detergent industries. The enzyme was purified 2.70 fold with specific activity of 1624U/mg in comparison to crude enzyme extract by using ammonium sulfate precipitation, dialysis and Sephadex G-75 column chromatography. The molecular mass of the enzyme was 27.2 kDa as judged by SDS–PAGE. The purified protease had a pH optimum of 8.5 and temperature optimum of 55°C. According to the inhibition profiles obtained with the various protease inhibitors, it was confirmed that the partially purified protease belongs to the serine protease type. The activity of partially purified enzyme was enhanced by calcium, magnesium, barium, potassium and manganese ions and strongly inhibited by mercury ion. In addition, the protease showed remarkable stability in the presence of 1% SDS; 1, 3 and 5% Triton X-100 and H<sub>2</sub>O<sub>2</sub>, which comprise the common bleach-based detergent formulation. The enzyme was found equally efficient to a commercial enzyme Oropon K (one of the commercial enzymes imported into Bangladesh for bating purpose) in bating of animal hide as proved by different comparative qualitative tests such as tensile strength, percent of elongation, stitch tears strength, water vapor permeability, grain crack strength and tongue tear  strength tests. In addition, the stability profile (pH, temperature and surfactants) and blood stain removal data also revealed its suitability for application in detergent industry.</p>

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