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A novel surfactant- and oxidation-stable alkaline protease from Vibrio metschnikovii DL 33–51

Paper ID Volume ID Publish Year Pages File Format Full-Text
36699 45142 2005 6 PDF Available
Title
A novel surfactant- and oxidation-stable alkaline protease from Vibrio metschnikovii DL 33–51
Abstract

A novel surfactant- and oxidation-stable alkaline protease from Vibrio metschnikovii DL 33–51 was purified using acetone precipitation, Q-sepharose ion exchange and Sephacryl S-100 gel filtration chromatographic techniques. The enzyme had a relative molecular weight of 29.5 kDa by SDS polyacrylamide gel electrophoresis. The optimal temperature and pH were found to be 60 °C and 12.0, respectively. The protease was stable in a pH range of 9.0–11.0. The half-lives of protease recorded at 50 and 60 °C were 7.5 h and 30 min, respectively. The enzyme activity could be strongly activated by several commercially available laboratory surfactants (Triton X-100, Tween-80) and bleaches (H2O2, sodium hypochlorite), and showed a valuable stability towards them when their concentrations ranged up to 1.0%. Enzyme activity was increased up to 19 and 18% by Mn2+ and Ba2+, respectively.

Keywords
Alkaline protease; Vibrio metschnikovii; Surfactant- and oxidation stable
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A novel surfactant- and oxidation-stable alkaline protease from Vibrio metschnikovii DL 33–51
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 40, Issue 6, May 2005, Pages 2167–2172
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us