ISSN:
0006-3592
Keywords:
subtilisin
;
organic solvents
;
nonaqueous enzymology
;
solutions and suspensions
;
secondary structure
;
Fourier-transform infrared (FTIR) spectroscopy
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Additional Material:
1 Ill.
Type of Medium:
Electronic Resource
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