Abstract
Noncovalent complexes were formed by lyophilization of aqueous solutions containing horse liver alcohol dehydrogenase, NAD+ and a polymer [ethyl cellulose or poly(vinyl butyral)]. The complexes expressed higher specific catalytic activity in organic solvents as compared to a corresponding amount of enzyme deposited on to Celite or lyophilized enzyme powder. The noncovalent complexes were soluble in toluene. In butyl acetate and methyl t-butyl ether, suspensions of fine particles were formed.
Original language | English |
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Pages (from-to) | 877-882 |
Number of pages | 6 |
Journal | Biotechnology Letters |
Volume | 17 |
Issue number | 8 |
DOIs | |
Publication status | Published - 1995 Aug 1 |
Subject classification (UKÄ)
- Biocatalysis and Enzyme Technology