Rational enhancement of enzyme performance in organic solvents. Final technical report, 1992--1996

Technical Report · Tue Dec 31 04:00:00 EST 1996

DOI:https://doi.org/10.2172/307997· OSTI ID:307997

Klibanov, A M

This research focused on the following: the dependence of enzymatic activity of several model hydrolases in nonaqueous solvents; control of substrate selectivity of the protease subtilisin Carlsberg by the solvent; control of catalytic activity and enantioselectivity of this enzyme in organic solvents by immobilization support; lipase-catalyzed acylation of sugars in anhydrous hydrophobic media; the possibility of accelerating enzymatic processes in organic solvents by certain cosolvents; whether lipase catalysis in organic solvents can be enhanced by introducing interfaces in the in the reaction medium; the structure of proteins suspended in organic solvents; improving enzymatic enantioselectivity in organic solvents; analyzing the plunge in enzymatic activity upon replacing water with organic solvents; and the structural basis for the phenomenon of molecular memory of imprinted proteins in organic solvents.

• Research Organization: Massachusetts Inst. of Tech., Cambridge, MA (United States)
• Sponsoring Organization: USDOE Assistant Secretary for Energy Efficiency and Renewable Energy, Washington, DC (United States)
• DOE Contract Number: FG36-92CH10518
• OSTI ID: 307997
• Report Number(s): DOE/CH/10518--T1; ON: DE99001583
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
BIOTECHNOLOGY
ENZYME ACTIVITY
HYDROLASES
LIPASES
ORGANIC SOLVENTS
PEPTIDE HYDROLASES
PROGRESS REPORT
PROTEIN STRUCTURE