On enzymatic activity in organic solvents as a function of enzyme history

Journal Article · Fri Mar 20 04:00:00 EST 1998 · Biotechnology and Bioengineering

DOI:https://doi.org/10.1002/(SICI)1097-0290(19980320)57:6<746::AID-BIT12>3.0.CO;2-5· OSTI ID:619420

Ke, T; Klibanov, A M ^[1]

---

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

Catalytic activities of {alpha}-chymotrypsin and subtilisin Carlsberg in various hydrous organic solvents were measured as a function of how the enzyme suspension had been prepared. In one method, lyophilized enzyme was directly suspended in the solvent containing 1% water. In another, the enzyme was precipitated from its aqueous solution by a 100-fold dilution with an anhydrous solvent. In most cases, the reaction rate in a given nonaqueous enzymatic system strongly (up to an order of magnitude) depended on the mode of enzyme preparation. The magnitude of this dependence was markedly affected by the nature of the solvent and enzyme. A mechanistic hypothesis proposed to explain the observed dependencies was verified in additional experiments in which the water contents and enzyme history were further varied.

• Sponsoring Organization: Oak Ridge National Lab., TN (United States)
• OSTI ID: 619420
• Journal Information: Biotechnology and Bioengineering, Journal Name: Biotechnology and Bioengineering Journal Issue: 6 Vol. 57; ISSN BIBIAU; ISSN 0006-3592
• Country of Publication: United States
• Language: English

Related Subjects

56 BIOLOGY AND MEDICINE
APPLIED STUDIES
CHEMICAL PREPARATION
CHYMOTRYPSIN
ENZYME ACTIVITY
LYOPHILIZATION
METABOLISM
ORGANIC SOLVENTS
PEPTIDE HYDROLASES