[Bacillus subtilis protease: isolation, immobilization and properties]

Area of Science:

• Biochemistry
• Enzyme Technology
• Microbial Biotechnology

Background:

• Bacillus subtilis is a well-known source of industrially relevant enzymes.
• Proteases are widely used in various industries, necessitating stable enzyme preparations.
• Enzyme immobilization is a key strategy for improving enzyme stability and reusability.

Purpose of the Study:

• To optimize the production and purification of protease from Bacillus subtilis strain 3H.
• To immobilize the purified protease onto a polyglucin support.
• To enhance the stability of the immobilized protease using glutaraldehyde cross-linking.

Main Methods:

• Cultivation of Bacillus subtilis under optimized conditions for protease production.
• Purification of protease using gel chromatography and ultrafiltration.
• Immobilization of purified protease on polyglucin.
• Stabilization of immobilized protease via intramolecular cross-linking with glutaraldehyde.

Main Results:

• Protease was successfully produced and purified from Bacillus subtilis.
• The purified protease was effectively immobilized on polyglucin.
• Immobilized protease stabilized with glutaraldehyde exhibited superior stability compared to native protease or protease modified with polyglucin alone.

Conclusions:

• Optimized cultivation conditions facilitate efficient protease production in Bacillus subtilis.
• Enzyme immobilization on polyglucin, particularly when cross-linked with glutaraldehyde, significantly enhances protease stability.
• This stabilized immobilized protease holds potential for various industrial applications requiring robust enzymatic activity.