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Applied and Environmental Microbiology, February 2001, p. 942-947, Vol. 67, No. 2
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.2.942-947.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Role of Intermolecular Disulfide Bonds of the Organic Solvent-Stable PST-01 Protease in Its Organic Solvent Stability

Hiroyasu Ogino,* Takeshi Uchiho, Jyunko Yokoo, Reina Kobayashi, Rikiya Ichise, and Haruo Ishikawa

Department of Chemical Engineering, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan

Received 3 February 2000/Accepted 17 August 2000

The PST-01 protease is secreted by the organic solvent-tolerant microorganism Pseudomonas aeruginosa PST-01 and is stable in the presence of various organic solvents. Therefore, the PST-01 strain and the PST-01 protease are very useful for fermentation and reactions in the presence of organic solvents, respectively. The organic solvent-stable PST-01 protease has two disulfide bonds (between Cys-30 and Cys-58 and between Cys-270 and Cys-297) in its molecule. Mutant PST-01 proteases in which one or both of the disulfide bonds were deleted were constructed by site-directed mutagenesis, and the effect of the disulfide bonds on the activity and the various stabilities was investigated. The disulfide bond between Cys-270 and Cys-297 in the PST-01 protease was found to be essential for its activity. The disulfide bond between Cys-30 and Cys-58 played an important role in the organic solvent stability of the PST-01 protease.

* Corresponding author. Mailing address: Department of Chemical Engineering, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan. Phone: 81-722-54-9299. Fax: 81-722-54-9911. E-mail: ogino{at}chemeng.osakafu-u.ac.jp.

Applied and Environmental Microbiology, February 2001, p. 942-947, Vol. 67, No. 2
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.2.942-947.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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