Catalytic activity of noncovalent complexes of horse liver alcohol dehydrogenase, NAD+ and polymers, dissolved or suspended in organic solvents

Carmen Virto, Ingemar Svensson, Patrick Adlercreutz, Bo Mattiasson

    Research output: Contribution to journalArticlepeer-review

    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 languageEnglish
    Pages (from-to)877-882
    Number of pages6
    JournalBiotechnology Letters
    Volume17
    Issue number8
    DOIs
    Publication statusPublished - 1995 Aug 1

    Subject classification (UKÄ)

    • Biocatalysis and Enzyme Technology

    Fingerprint

    Dive into the research topics of 'Catalytic activity of noncovalent complexes of horse liver alcohol dehydrogenase, NAD+ and polymers, dissolved or suspended in organic solvents'. Together they form a unique fingerprint.

    Cite this