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[The properties of protease from Bacillus sphaericus C3-41]
Wei Sheng Wu Xue Bao = Acta Microbiologica Sinica
|February 24, 2001
Summary
This study details the production and purification of extracellular protease from Bacillus sphaericus. The enzyme exhibits optimal activity at pH 11.0 and 4°C, with notable stability and specific inhibition patterns.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Background:
- Bacillus sphaericus is a known source of microbial enzymes.
- Extracellular proteases play significant roles in microbial physiology and biotechnological applications.
- Understanding protease production dynamics is crucial for optimizing yields.
Purpose of the Study:
- To investigate the production kinetics of extracellular protease from Bacillus sphaericus C3-41.
- To purify and characterize the properties of the isolated protease.
- To determine the optimal conditions and stability of the enzyme.
Main Methods:
- Cultivation of Bacillus sphaericus C3-41 to study protease secretion phases.
- Enzyme purification using ammonium sulfate precipitation and Sephadex G-100 chromatography.
- Characterization of protease activity, stability, and inhibition profiles.
Main Results:
- Protease secretion initiated during the exponential growth phase, peaking in the early sporangium phase.
- Purified protease showed a specific activity of 6741.5 U/mg protein and a molecular weight of 42,000 Da.
- Optimal activity observed at pH 11.0 and 4°C; stable between pH 5.0-12.0.
- Enzyme activity was inhibited by PMSF, EDTA, and divalent metal ions (Al3+, Hg2+, Fe3+, Cu2+, Fe2+), but stabilized by Ca2+.
Conclusions:
- Bacillus sphaericus C3-41 produces a highly active alkaline protease.
- The enzyme's characteristics suggest potential applications in industrial processes requiring alkaline conditions.
- Further research can focus on optimizing production and exploring specific biotechnological uses.