Effect of support material and enzyme pretreatment on enantioselectivity of immobilized subtilisin in organic solvents

Journal Article · Sun Nov 20 00:00:00 EST 1994 · Biotechnology and Bioengineering; (United States)

DOI:https://doi.org/10.1002/bit.260441015· OSTI ID:6904291

Orsat, B; Klibanov, A M ^[1]; Drtina, G J; Williams, M G ^[2]

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1. Massachusetts Inst. of Technology, Cambridge, MA (United States). Dept. of Chemistry
2. 3M, St. Paul, MN (United States)

Subtilisin Carlsberg was covalently attached to five macroporous acrylic supports of varying aquaphilicity (a measure of hydrophilicity). Kinetic parameters of the transesterification of S and R enantiomers of sec-phenethyl alcohol with vinyl butyrate, catalyzed by various immobilized subtilisins, were determined in anhydrous dioxane and acetonitrile. Enzyme enantioselectivity in acetonitrile, but not in dioxane, correlated with the aquaphilicity of the support; a mechanistic rationale for this phenomenon was proposed. Although the catalytic activity of immobilized subtilisin in anhydrous solvents strongly depended on enzyme pretreatment, the enantioselectivity was essential conserved.

• OSTI ID: 6904291
• Journal Information: Biotechnology and Bioengineering; (United States), Vol. 44:10; ISSN 0006-3592
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PEPTIDE HYDROLASES
BIOCHEMICAL REACTION KINETICS
IMMOBILIZED ENZYMES
RESPONSE MODIFYING FACTORS
SUBSTRATES
ENZYMES
HYDROLASES
KINETICS
ORGANIC COMPOUNDS
PROTEINS
REACTION KINETICS
550200* - Biochemistry