Open AccessEnzyme function in organic solvents
Author(s) -
GUPTA Munishwar N.
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb19823.x
Subject(s) - thermostability , biocatalysis , protein engineering , anhydrous , thermal stability , chemistry , catalysis , aqueous solution , polymer , organic chemistry , enzyme catalysis , immobilized enzyme , enzyme , catalytic efficiency , chemical engineering , combinatorial chemistry , ionic liquid , engineering
Enzyme catalysis in organic solvents is being increasingly used for a variety of applications. Of special interest are the cases in which the medium is predominantly non‐aqueous and contains little water. A display of enzyme activity, even in anhydrous solvents (water <0.02% by vol.), perhaps reflects that the minimum necessity for water is for forming bonds with polar amino acids on the enzyme surface. The rigidity of enzyme structure at such low water content results in novel substrate specificities, pH memory and the possibility of techniques such as molecular imprinting. Limited data indicates that, while enhanced thermal stability invariably results, the optimum temperature for catalysis may not change. If true in general, this enhanced thermostability would have extremely limited benefits. Medium engineering and biocatalyst engineering are relevant techniques to improve the efficiency and stability of enzymes in such low water systems. Most promising, as part of the latter, is the technique of protein engineering. Finally, this review provides illustrations of applications of such systems in the diverse areas of organic synthesis, analysis and polymer chemistry.