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International Journal of Current Microbiology and Applied Sciences (IJCMAS)
IJCMAS is now DOI (CrossRef) registered Research Journal. The DOIs are assigned to all published IJCMAS Articles.
Index Copernicus ICI Journals Master List 2018 - IJCMAS--ICV 2018: 95.39 For more details click here
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National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2020)
[Effective from January 1, 2020]
For more details click here

ICV 2018: 95.39
Index Copernicus ICI Journals Master List 2018 - IJCMAS--ICV 2018: 95.39
For more details click here

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Original Research Articles

PRINT ISSN : 2319-7692
Online ISSN : 2319-7706
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcmas@gmail.com / submit@ijcmas.com
Editor-in-chief: Dr.M.Prakash
Index Copernicus ICV 2018: 95.39
NAAS RATING 2020: 5.38

Int.J.Curr.Microbiol.App.Sci.2018.7(8): 587-600
DOI: https://doi.org/10.20546/ijcmas.2018.708.064


Production, Partial Purification, Characterization and Detergent Compatibility of Alkaline Protease from Soil Isolate Bacillus cereus AG1
Yogesh Patel1*, Akshaya Gupte2 and Shilpa Gupte3
1Department of Microbiology, College of Basic Science and Humanities, Sardarkrushinagar Dantiwada Agricultural University (SDAU), Sardarkrushinagar, 385 506, Gujarat, India
2Department of Microbiology, Natubhai V. Patel College of Pure and Applied Sciences, Vallabh Vidyanagar, Anand, 388 120, Gujarat, India
3Ashok and Rita Patel Institute of Integrated Study and Research in Biotechnology and Allied Sciences, New Vallabh Vidyanagar, Anand, 388 120, Gujarat, India
*Corresponding author
Abstract:

Proteases are one of the most important groups of enzymes with wide range of industrial applications. The soil isolate Bacillus cereusAG1 produced alkaline protease under submerged cultivation condition. Maximum production of enzyme was achieved at pH 10.0 and temperature 30oC at 120 rpm. The supplementation of fructose as carbon source and combination of beef extract, yeast extract and peptone as nitrogen source improved enzyme production by 1.39 times. Partial purification of enzyme by dialysis exhibited 3.07 fold purification with 60.15% yield. The characterization of partially purified alkaline protease displayed optimum activity at pH 10.0, temperature 50oC with casein as the most suitable substrate. Mmaximum enzyme activity 250 U ml-1and Michaelis constant (0.28%) of alkaline protease were obtained by varying casein concentration (1.0-2.0% w/v). The alkaline protease activity was enhanced in the presence of Ca+2, while Na+ and Hg+2 inhibited the enzyme activity. The enzyme retained 59.92% activity in the presence of 5.0 mM EDTA. The detergent stability and compatibility of alkaline protease suggest its potential utility as cleaning additive.


Keywords: Alkaline protease, Bacillus cereus AG1, Optimization, Enzyme activity, Detergent compatibility
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How to cite this article:

Yogesh Patel, Akshaya Gupte and Shilpa Gupte. 2018. Production, Partial Purification, Characterization and Detergent Compatibility of Alkaline Protease from Soil Isolate Bacillus cereus AG1.Int.J.Curr.Microbiol.App.Sci. 7(8): 587-600. doi: https://doi.org/10.20546/ijcmas.2018.708.064