Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media
Separation of racemic mixtures is a formidable task and various approaches have been suggested. The resolution of R(−)-mandelic acid, which is used as an intermediate in pharmaceutical and drug industry, from a racemic mixture was studied in non-aqueous media via lipase catalyzed hydrolysis of RS(∓)...
Main Authors: | , |
---|---|
Format: | Article in Journal/Newspaper |
Language: | unknown |
Published: |
Elsevier Science
2004
|
Subjects: | |
Online Access: | http://repository.ias.ac.in/111772/ http://www.sciencedirect.com/science/article/pii/S1369703X03002936 |
id |
ftindianacasci:oai:repository.ias.ac.in:111772 |
---|---|
record_format |
openpolar |
spelling |
ftindianacasci:oai:repository.ias.ac.in:111772 2023-05-15T14:15:28+02:00 Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media Yadav, Ganapati D. Sivakumar, P. 2004-07-15 http://repository.ias.ac.in/111772/ http://www.sciencedirect.com/science/article/pii/S1369703X03002936 unknown Elsevier Science Yadav, Ganapati D. Sivakumar, P. (2004) Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media Biochemical Engineering Journal, 19 (2). pp. 101-107. ISSN 1369-703X T Technology (General) Article PeerReviewed 2004 ftindianacasci 2017-09-22T22:09:35Z Separation of racemic mixtures is a formidable task and various approaches have been suggested. The resolution of R(−)-mandelic acid, which is used as an intermediate in pharmaceutical and drug industry, from a racemic mixture was studied in non-aqueous media via lipase catalyzed hydrolysis of RS(∓)-methyl mandelate. Novozym 435 (component B of the lipase from Candida antartica), lipozyme RM IM (Rhizomucor miehei lipase) and lipozyme TL IM (Thermomyces lanuginosus lipase) were screened for their activity and selectivity to get R(−)-mandelic acid. Novozym 435 was found to be the most effective in hydrolysis of R(−)-methyl mandelate with an optical purity of 78% at the end of 24 h. Effects of various process parameters such as speed of agitation, catalyst loading, substrate concentration, product concentration and temperature were studied. The ordered bi–bi mechanism with inhibition by both R(−)-methyl mandelate (substrate) and R(−)-mandelic acid (product) was found to fit the initial rate data very well and the kinetic constants were determined. Article in Journal/Newspaper antartic* Indian Academy of Sciences: Publication of Fellows |
institution |
Open Polar |
collection |
Indian Academy of Sciences: Publication of Fellows |
op_collection_id |
ftindianacasci |
language |
unknown |
topic |
T Technology (General) |
spellingShingle |
T Technology (General) Yadav, Ganapati D. Sivakumar, P. Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media |
topic_facet |
T Technology (General) |
description |
Separation of racemic mixtures is a formidable task and various approaches have been suggested. The resolution of R(−)-mandelic acid, which is used as an intermediate in pharmaceutical and drug industry, from a racemic mixture was studied in non-aqueous media via lipase catalyzed hydrolysis of RS(∓)-methyl mandelate. Novozym 435 (component B of the lipase from Candida antartica), lipozyme RM IM (Rhizomucor miehei lipase) and lipozyme TL IM (Thermomyces lanuginosus lipase) were screened for their activity and selectivity to get R(−)-mandelic acid. Novozym 435 was found to be the most effective in hydrolysis of R(−)-methyl mandelate with an optical purity of 78% at the end of 24 h. Effects of various process parameters such as speed of agitation, catalyst loading, substrate concentration, product concentration and temperature were studied. The ordered bi–bi mechanism with inhibition by both R(−)-methyl mandelate (substrate) and R(−)-mandelic acid (product) was found to fit the initial rate data very well and the kinetic constants were determined. |
format |
Article in Journal/Newspaper |
author |
Yadav, Ganapati D. Sivakumar, P. |
author_facet |
Yadav, Ganapati D. Sivakumar, P. |
author_sort |
Yadav, Ganapati D. |
title |
Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media |
title_short |
Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media |
title_full |
Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media |
title_fullStr |
Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media |
title_full_unstemmed |
Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media |
title_sort |
enzyme-catalysed optical resolution of mandelic acid via rs(∓)-methyl mandelate in non-aqueous media |
publisher |
Elsevier Science |
publishDate |
2004 |
url |
http://repository.ias.ac.in/111772/ http://www.sciencedirect.com/science/article/pii/S1369703X03002936 |
genre |
antartic* |
genre_facet |
antartic* |
op_relation |
Yadav, Ganapati D. Sivakumar, P. (2004) Enzyme-catalysed optical resolution of mandelic acid via RS(∓)-methyl mandelate in non-aqueous media Biochemical Engineering Journal, 19 (2). pp. 101-107. ISSN 1369-703X |
_version_ |
1766287843420798976 |