Premium
Correlation between catalytic activity and secondary structure of subtilisin dissolved in organic solvents
Author(s) -
Xu Kui,
Griebenow Kai,
Klibanov Alexander M.
Publication year - 1997
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19971205)56:5<485::aid-bit2>3.0.co;2-e
Subject(s) - subtilisin , chemistry , solvent , aqueous solution , catalysis , fourier transform infrared spectroscopy , protein secondary structure , enzyme , organic chemistry , chromatography , nuclear chemistry , chemical engineering , biochemistry , engineering
Fourier‐transform infrared (FTIR) spectroscopy has been used to quantify the α‐helix and β‐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 α‐helix or β‐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. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 485–491, 1997.