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- W2037661640 abstract "The γ-isoenzyme of pig liver esterase (rPLE) was produced recombinantly by expression in Pichia pastoris. A comparison of rPLE with commercial preparations of crude PLE revealed significant differences in the kinetic resolution of a series of acetates of secondary alcohols. With rPLE substantially higher enantioselectivities were observed in the hydrolysis of (R,S)-1-phenyl-3-butyl acetate, (R,S)-1-phenyl-2-propyl acetate, (R,S)-1-phenyl-2-pentyl acetate, and (R,S)-1-phenyl-2-butyl acetate. For the first two compounds, also an inversed stereopreference was found. This change in substrate specificity can be related to varying contents of the γ-isoenzyme in commercial PLE preparations and the presence of further isoenzymes with different properties." @default.
- W2037661640 created "2016-06-24" @default.
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- W2037661640 date "2002-12-01" @default.
- W2037661640 modified "2023-09-27" @default.
- W2037661640 title "Substrate specificity of the γ-isoenzyme of recombinant pig liver esterase towards acetates of secondary alcohols" @default.
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- W2037661640 doi "https://doi.org/10.1016/s1381-1177(02)00159-5" @default.
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