eprintid: 54
rev_number: 2
eprint_status: archive
userid: 1
dir: disk0/00/00/00/54
datestamp: 2023-11-09 15:10:37
lastmod: 2023-11-09 15:10:37
status_changed: 2023-11-09 15:09:41
type: article
metadata_visibility: show
creators_name: Ujang, Z.
creators_name: Husain, W.H.
creators_name: Seng, M.C.
creators_name: Rashid, A.H.A.
title: The kinetic resolution of 2-(4-chlorophenoxy) propionic acid using Candida rugosa lipase
ispublished: pub
keywords: Candida; Candida rugosa; Candida rugosa
note: cited By 36
abstract: The effect of solvent, operating temperature, enzyme concentration and immobilization on activity and enantioselectivity of a Candida rugosa lipase for the kinetic resolution of ±2-(4-chlorophenoxy) propionic acid with 1-butanol in organic solvents was studied. The crude enzyme powder gave more than 50 conversion and with an enantiomeric excess (ee) of 100 for the remaining S-acid at 40°C with carbon tetrachloride as the solvent. Higher enantioselectivities were obtained when the reactions were performed at temperatures between 30 and 40°C and at lower water activities, aw. Immobilization of the lipase onto various types of support results in loss of activity and selectivity. The best results was obtained with the enzyme preparation immobilized onto silica gel. This gave 33 overall conversion and an ee of 46 for the S-acid. Continuous resolution process via a packed bed reactor resulted in an overall conversion of around 50 and 100 ee for the S enantiomer. © 2003 Elsevier Science Ltd. All rights reserved.
date: 2003
publisher: Elsevier BV
official_url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038274857&doi=10.1016%2fS0032-9592%2803%2900039-6&partnerID=40&md5=4d5e2e6c02f7366ae88ee93f05a57255
id_number: 10.1016/S0032-9592(03)00039-6
full_text_status: none
publication: Process Biochemistry
volume: 38
number: 10
pagerange: 1483-1488
refereed: TRUE
issn: 13595113
citation:   Ujang, Z. and Husain, W.H. and Seng, M.C. and Rashid, A.H.A.  (2003) The kinetic resolution of 2-(4-chlorophenoxy) propionic acid using Candida rugosa lipase.  Process Biochemistry, 38 (10).  pp. 1483-1488.  ISSN 13595113