Effect of support material and enzyme pretreatment on enantioselectivity of immobilized subtilisin in organic solvents
Journal Article
·
· Biotechnology and Bioengineering; (United States)
- Massachusetts Inst. of Technology, Cambridge, MA (United States). Dept. of Chemistry
- 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), Journal Name: Biotechnology and Bioengineering; (United States) Vol. 44:10; ISSN BIBIAU; ISSN 0006-3592
- Country of Publication:
- United States
- Language:
- English
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