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Correlation between catalytic activity and secondary structure of subtilisin dissolved in organic solvents

✍ Scribed by Kui Xu; Kai Griebenow; Alexander M. Klibanov


Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
73 KB
Volume
56
Category
Article
ISSN
0006-3592

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✦ Synopsis


Fourier-transform infrared (FTIR) spectroscopy has been used to quantify the alpha-helix and beta-sheet contents of subtilisin Carlsberg dissolved in several nonaqueous, as well as aqueous, solvents. Independently, the catalytic activity of the enzyme has been measured in the same solvents. While our previous FTIR studies revealed no connection between the secondary structure and enzymatic activity for subtilisin suspended in various organic solvents, a very different situation is observed herein for the dissolved enzyme. Specifically, if either the alpha-helix or beta-sheet content in a given solvent is higher or lower than in water, no appreciable enzymatic catalysis is observed. Conversely, when the secondary structure of subtilisin dissolved in a given nonaqueous solvent is similar to that in water, so is the enzymatic activity. (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 485-491, 1997.


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