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

doi:10.1007/BF00129022

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

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Sammanfattning

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.

Originalspråk	engelska
Sidor (från-till)	877-882
Antal sidor	6
Tidskrift	Biotechnology Letters
Volym	17
Nummer	8
DOI	https://doi.org/10.1007/BF00129022
Status	Published - 1995 aug. 1

Ämnesklassifikation (UKÄ)

Biokatalys och enzymteknik

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10.1007/BF00129022

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

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.",

author = "Carmen Virto and Ingemar Svensson and Patrick Adlercreutz and Bo Mattiasson",

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AU - Mattiasson, Bo

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N2 - 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.

AB - 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.

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