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An overview on fermentation, downstream processing and properties of microbial alkaline proteases
1Department of Microbiology, University of Delhi South Campus, Benito Juarez Marg, New Delhi 110 021, India. ranigupta15@rediffmail.com
Applied Microbiology and Biotechnology
|December 6, 2002
Summary
Microbial alkaline proteases, mainly from Bacillus species, are crucial for the detergent industry. Optimizing fermentation, purification, and assay methods is key for developing efficient industrial enzyme processes.
Area of Science:
- Biotechnology
- Enzymology
- Industrial Microbiology
Background:
- Microbial alkaline proteases are vital industrial enzymes, dominating the enzyme market and detergent industry.
- Bacillus species are the primary source of commercially exploited extracellular proteases.
- Understanding fermentation, purification, and biocatalyst properties is essential for industrial enzyme process development.
Purpose of the Study:
- To highlight the importance of microbial alkaline proteases in industry.
- To discuss fermentation parameters, purification strategies, and biocatalyst properties.
- To emphasize the need for updated assay protocols for novel biocatalyst generation.
Main Methods:
- Review of literature on microbial protease production and characterization.
- Discussion of fermentation control (C/N ratio, fed-batch, continuous culture).
- Overview of purification techniques (concentration, chromatography, aqueous two-phase systems).
Main Results:
- Microbial alkaline proteases constitute a major share of the enzyme market, especially in detergents.
- Bacillus sp. are dominant in industrial protease production.
- Alkaline proteases exhibit optimal activity at pH 8-12 and temperatures of 50-70°C, with some exceptions.
Conclusions:
- Efficient industrial enzyme processes require comprehensive knowledge of fermentation, purification, and protease characteristics.
- Development of micro/nano-scale assay protocols is important for generating improved biocatalysts.
- Crystallization aids in understanding the molecular structure and homology of industrially significant proteases.
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