Lipase-catalyzed dynamic resolution of naproxen thioester by thiotransesterification in isooctane

Chun Sheng Chang; Shau Wei Tsai

doi:10.1016/S1369-703X(99)00022-4

Lipase-catalyzed dynamic resolution of naproxen thioester by thiotransesterification in isooctane

Chun Sheng Chang
, Shau Wei Tsai^*

^*Corresponding author for this work

National Cheng Kung University

Research output: Contribution to journal › Journal Article › peer-review

14 Scopus citations

Abstract

A lipase-catalyzed enantioselective thiotransesterification between (R,S)-naproxen thioester and 4-morpholine ethanol under in situ racemization of the (R)-thioester by trioctylamine in isooctane was developed. More than 65% yield and 95% enantiomeric excess for the desired (S)-ester product were obtained. Maximum in the initial rate was found at the alcohol concentration of ca. 5 mM, which indicates the alcohol to be an enzyme inhibitor. The initial hydrolysis rate and the yield of the undesired (S)-naproxen were suppressed by increasing the alcohol concentration or employing an immobilized lipase containing less water than the free enzyme.

Original language	English
Pages (from-to)	239-242
Number of pages	4
Journal	Biochemical Engineering Journal
Volume	3
Issue number	3
DOIs	https://doi.org/10.1016/S1369-703X(99)00022-4
State	Published - 06 1999
Externally published	Yes

Keywords

Dynamic resolution
Enzyme biocatalysis
Lipase
Naproxen ester
Thiotransesterification

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10.1016/S1369-703X(99)00022-4

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title = "Lipase-catalyzed dynamic resolution of naproxen thioester by thiotransesterification in isooctane",

abstract = "A lipase-catalyzed enantioselective thiotransesterification between (R,S)-naproxen thioester and 4-morpholine ethanol under in situ racemization of the (R)-thioester by trioctylamine in isooctane was developed. More than 65\% yield and 95\% enantiomeric excess for the desired (S)-ester product were obtained. Maximum in the initial rate was found at the alcohol concentration of ca. 5 mM, which indicates the alcohol to be an enzyme inhibitor. The initial hydrolysis rate and the yield of the undesired (S)-naproxen were suppressed by increasing the alcohol concentration or employing an immobilized lipase containing less water than the free enzyme.",

keywords = "Dynamic resolution, Enzyme biocatalysis, Lipase, Naproxen ester, Thiotransesterification",

author = "Chang, \{Chun Sheng\} and Tsai, \{Shau Wei\}",

year = "1999",

month = jun,

doi = "10.1016/S1369-703X(99)00022-4",

language = "英语",

volume = "3",

pages = "239--242",

journal = "Biochemical Engineering Journal",

issn = "1369-703X",

publisher = "Elsevier B.V.",

number = "3",

}

TY - JOUR

T1 - Lipase-catalyzed dynamic resolution of naproxen thioester by thiotransesterification in isooctane

AU - Chang, Chun Sheng

AU - Tsai, Shau Wei

PY - 1999/6

Y1 - 1999/6

N2 - A lipase-catalyzed enantioselective thiotransesterification between (R,S)-naproxen thioester and 4-morpholine ethanol under in situ racemization of the (R)-thioester by trioctylamine in isooctane was developed. More than 65% yield and 95% enantiomeric excess for the desired (S)-ester product were obtained. Maximum in the initial rate was found at the alcohol concentration of ca. 5 mM, which indicates the alcohol to be an enzyme inhibitor. The initial hydrolysis rate and the yield of the undesired (S)-naproxen were suppressed by increasing the alcohol concentration or employing an immobilized lipase containing less water than the free enzyme.

AB - A lipase-catalyzed enantioselective thiotransesterification between (R,S)-naproxen thioester and 4-morpholine ethanol under in situ racemization of the (R)-thioester by trioctylamine in isooctane was developed. More than 65% yield and 95% enantiomeric excess for the desired (S)-ester product were obtained. Maximum in the initial rate was found at the alcohol concentration of ca. 5 mM, which indicates the alcohol to be an enzyme inhibitor. The initial hydrolysis rate and the yield of the undesired (S)-naproxen were suppressed by increasing the alcohol concentration or employing an immobilized lipase containing less water than the free enzyme.

KW - Dynamic resolution

KW - Enzyme biocatalysis

KW - Lipase

KW - Naproxen ester

KW - Thiotransesterification

UR - https://www.scopus.com/pages/publications/0033020859

U2 - 10.1016/S1369-703X(99)00022-4

DO - 10.1016/S1369-703X(99)00022-4

M3 - 文章

AN - SCOPUS:0033020859

SN - 1369-703X

VL - 3

SP - 239

EP - 242

JO - Biochemical Engineering Journal

JF - Biochemical Engineering Journal

IS - 3

ER -

Lipase-catalyzed dynamic resolution of naproxen thioester by thiotransesterification in isooctane

Abstract

Keywords

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