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

Journal Article · Fri Dec 05 04:00:00 EST 1997 · Biotechnology and Bioengineering

DOI:https://doi.org/10.1002/(SICI)1097-0290(19971205)56:5<485::AID-BIT2>3.3.CO;2-V· OSTI ID:566370

Xu, K; Griebenow, K; Klibanov, A M ^[1]

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1. Massachusetts Inst. of Tech., Cambridge, MA (United States). Dept. of Chemistry

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 their 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.

• OSTI ID: 566370
• Journal Information: Biotechnology and Bioengineering, Journal Name: Biotechnology and Bioengineering Journal Issue: 5 Vol. 56; ISSN BIBIAU; ISSN 0006-3592
• Country of Publication: United States
• Language: English

Related Subjects

54 ENVIRONMENTAL SCIENCES
BIODEGRADATION
ENZYME ACTIVITY
FOURIER TRANSFORMATION
MOLECULAR STRUCTURE
ORGANIC SOLVENTS
REMEDIAL ACTION
SERINE PROTEINASES