Production and characterization of thermostable alkaline protease of Bacillus subtilis (ATCC 6633) from optimized solid‐state fermentation. (15th January 2015)
- Record Type:
- Journal Article
- Title:
- Production and characterization of thermostable alkaline protease of Bacillus subtilis (ATCC 6633) from optimized solid‐state fermentation. (15th January 2015)
- Main Title:
- Production and characterization of thermostable alkaline protease of Bacillus subtilis (ATCC 6633) from optimized solid‐state fermentation
- Authors:
- Chatterjee, Joyee
Giri, Sudipta
Maity, Sujan
Sinha, Ankan
Ranjan, Ashish
Rajshekhar,
Gupta, Suvroma - Abstract:
- <abstract abstract-type="main"> <title>Abstract</title> <p>Proteases are the most important group of enzymes utilized commercially in various arenas of industries, such as food, detergent, leather, dairy, pharmaceutical, diagnostics, and waste management, accounting for nearly 20% of the world enzyme market. Microorganisms of specially <italic>Bacillus</italic> genera serve as a vast repository of diverse set of industrially important enzymes and utilized for the large‐scale enzyme production using a fermentation technology. Approximately 30%–40% of the cost of industrial enzymes originates from the cost of the growth medium. This study is attempted to produce protease from <italic>Bacillus subtilis</italic> (ATCC 6633) after optimization of various process parameters with the aid of solid‐state fermentation using a cheap nutrient source such as wheat bran. <italic>B. subtilis</italic> (ATCC 6633) produces proteases of molecular weight 36 and 20 kDa, respectively, in the fermented medium as evident from SDS zymogram. Alkaline protease activity has been detected with optimum temperature at 50 °C and is insensitive to ethylenediaminetetraacetic acid. This thermostable alkaline protease exhibits dual pH optimum at 7 and 10 with moderate pH stability at alkaline pH range. It preserves its activity in the presence of detergent such as SDS, Tween 20, and Triton X‐100 and may be considered as an effective additive to detergent formulation with some industrial importance.</p><abstract abstract-type="main"> <title>Abstract</title> <p>Proteases are the most important group of enzymes utilized commercially in various arenas of industries, such as food, detergent, leather, dairy, pharmaceutical, diagnostics, and waste management, accounting for nearly 20% of the world enzyme market. Microorganisms of specially <italic>Bacillus</italic> genera serve as a vast repository of diverse set of industrially important enzymes and utilized for the large‐scale enzyme production using a fermentation technology. Approximately 30%–40% of the cost of industrial enzymes originates from the cost of the growth medium. This study is attempted to produce protease from <italic>Bacillus subtilis</italic> (ATCC 6633) after optimization of various process parameters with the aid of solid‐state fermentation using a cheap nutrient source such as wheat bran. <italic>B. subtilis</italic> (ATCC 6633) produces proteases of molecular weight 36 and 20 kDa, respectively, in the fermented medium as evident from SDS zymogram. Alkaline protease activity has been detected with optimum temperature at 50 °C and is insensitive to ethylenediaminetetraacetic acid. This thermostable alkaline protease exhibits dual pH optimum at 7 and 10 with moderate pH stability at alkaline pH range. It preserves its activity in the presence of detergent such as SDS, Tween 20, and Triton X‐100 and may be considered as an effective additive to detergent formulation with some industrial importance.</p> </abstract> … (more)
- Is Part Of:
- Biotechnology and applied biochemistry. Volume 62:Number 5(2015)
- Journal:
- Biotechnology and applied biochemistry
- Issue:
- Volume 62:Number 5(2015)
- Issue Display:
- Volume 62, Issue 5 (2015)
- Year:
- 2015
- Volume:
- 62
- Issue:
- 5
- Issue Sort Value:
- 2015-0062-0005-0000
- Page Start:
- 709
- Page End:
- 718
- Publication Date:
- 2015-01-15
- Subjects:
- Biotechnology -- Periodicals
Biochemical engineering -- Periodicals
Biochemistry -- Periodicals
Biochemistry -- Periodicals
Genetic Techniques -- Periodicals
Microbiological Techniques -- Periodicals
660.6 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1470-8744 ↗
http://www.babonline.org/ ↗
http://onlinelibrary.wiley.com/ ↗
http://bab.portlandpress.com/ ↗
http://bab.portlandpress.co.uk/ ↗ - DOI:
- 10.1002/bab.1309 ↗
- Languages:
- English
- ISSNs:
- 0885-4513
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2089.848000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3010.xml