Thermostable Protease from Thermophilic Bacteria

1. The effect of temperature on the conformation of the protease from Bacillus thermoproteolyticus was examined. 2. The thermostable enzyme is stable at room temperature against such denaturing reagents as urea, alcohol, and detergent. 3. However, these reagents accelerate the denaturation of the en...

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Bibliographic Details
Published in:The Journal of biological chemistry 1967-02, Vol.242 (3), p.509-515
Main Author: Ohta, Yumiko
Format: Article
Language:English
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Summary:1. The effect of temperature on the conformation of the protease from Bacillus thermoproteolyticus was examined. 2. The thermostable enzyme is stable at room temperature against such denaturing reagents as urea, alcohol, and detergent. 3. However, these reagents accelerate the denaturation of the enzyme by heat. 4. The effect of pH on the stability of the enzyme was examined, and it is suggested that the abnormally ionizing tyrosine residues contribute to the maintenance of the enzyme structure. 5. It is deduced from the physicochemical properties of the heated enzyme that the abnormal ionization and the Cotton effect of the tyrosine residues are due primarily to the hydrogen bonding of the phenol group.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(18)96302-7