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Asymmetric hydrolysis of dimethyl 3-phenylglutarate catalyzed by Lecitase Ultra®: Effect of the immobilization protocol on its catalytic properties

Paper ID Volume ID Publish Year Pages File Format Full-Text
17662 42687 2008 6 PDF Available
Title
Asymmetric hydrolysis of dimethyl 3-phenylglutarate catalyzed by Lecitase Ultra®: Effect of the immobilization protocol on its catalytic properties
Abstract

The asymmetric hydrolysis of dimethyl 3-phenylglutarate (1) by different immobilized preparations of a phospholipase A1 (Lecitase Ultra (LECI)) at pH 7 and 25 °C has been studied. Agarose beads coated with octyl, cyanogen bromide (CNBr), polyethylenimine (PEI) or glyoxyl groups were used as supports for the immobilization of LECI. The different derivatives behaved very differently in terms of activity, discrimination between 1 and methyl 3-phenylglutarate (2) resulting from the hydrolysis of 1, enantioselectivity (in the hydrolysis of 1 to produce R or S-2) and enantiospecificity in the hydrolysis of R-2 and S-2. Using 1 mM of 1, CNBr-LECI showed the highest activity (13 × 10−3 μmol/min mg protein) while octyl-LECI was about 20 times less active. All the enzyme preparations mainly produced (S)-2, but with different enantioselectivity. CNBr-Lecitase was the most enantioselective, producing the S-2 10 fold more rapidly than the R-2, while octyl-Lecitase gave only half of that difference.LECI adsorbed on octyl-agarose allowed to get a yield up to 99% of S-2 (ee was 66%). The reaction stopped in the monoester and no isomer of this compound was further hydrolyzed by the enzyme. However, when the reaction was catalyzed by the other immobilized LECI preparations, the enzyme was able to hydrolyze mainly the minority isomer, permitting to improve the ee of the remaining S-2. The best results were obtained using CNBr-LECI, which gave (S)-methyl-3-phenylglutarate with a yield of 80% and an ee exceeding 99%.

Keywords
Immobilized phospholipases; Asymmetric hydrolysis; Phenyl glutarate; Modulation of enzyme properties; Enzyme specificity; Enzyme selectivity
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Asymmetric hydrolysis of dimethyl 3-phenylglutarate catalyzed by Lecitase Ultra®: Effect of the immobilization protocol on its catalytic properties
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 43, Issue 7, 10 December 2008, Pages 531–536
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us