Lipase catalyse glycerolysis for kinetic resolution of racemates

C. Dlugy; A. Wolfson

doi:10.1007/s00449-007-0128-x

Lipase catalyse glycerolysis for kinetic resolution of racemates

C. Dlugy
, A. Wolfson

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

23 Scopus citations

Abstract

Candida antarctica lipase B catalyzed kinetic resolution of representative secondary alcohols, esters, and amine was successfully performed using triacetin or glycerol as solvents and acyl donor/acceptor. High conversions and enantioselectivities were achieved and the product was easily separated by simple extraction with diethyl ether.

Original language	English
Pages (from-to)	327-330
Number of pages	4
Journal	Bioprocess and Biosystems Engineering
Volume	30
Issue number	5
DOIs	https://doi.org/10.1007/s00449-007-0128-x
State	Published - 1 Sep 2007
Externally published	Yes

Keywords

Kinetic resolution
Lipase
Transesterification

ASJC Scopus subject areas

Biotechnology
Bioengineering

Access to Document

10.1007/s00449-007-0128-x

Cite this

@article{456d4ec372964c35945e23a0a0e1b632,

title = "Lipase catalyse glycerolysis for kinetic resolution of racemates",

abstract = "Candida antarctica lipase B catalyzed kinetic resolution of representative secondary alcohols, esters, and amine was successfully performed using triacetin or glycerol as solvents and acyl donor/acceptor. High conversions and enantioselectivities were achieved and the product was easily separated by simple extraction with diethyl ether.",

keywords = "Kinetic resolution, Lipase, Transesterification",

author = "C. Dlugy and A. Wolfson",

year = "2007",

month = sep,

day = "1",

doi = "10.1007/s00449-007-0128-x",

language = "English",

volume = "30",

pages = "327--330",

journal = "Bioprocess and Biosystems Engineering",

issn = "1615-7591",

publisher = "Springer Science and Business Media Deutschland GmbH",

number = "5",

}

TY - JOUR

T1 - Lipase catalyse glycerolysis for kinetic resolution of racemates

AU - Dlugy, C.

AU - Wolfson, A.

PY - 2007/9/1

Y1 - 2007/9/1

N2 - Candida antarctica lipase B catalyzed kinetic resolution of representative secondary alcohols, esters, and amine was successfully performed using triacetin or glycerol as solvents and acyl donor/acceptor. High conversions and enantioselectivities were achieved and the product was easily separated by simple extraction with diethyl ether.

AB - Candida antarctica lipase B catalyzed kinetic resolution of representative secondary alcohols, esters, and amine was successfully performed using triacetin or glycerol as solvents and acyl donor/acceptor. High conversions and enantioselectivities were achieved and the product was easily separated by simple extraction with diethyl ether.

KW - Kinetic resolution

KW - Lipase

KW - Transesterification

UR - https://www.scopus.com/pages/publications/35748957517

U2 - 10.1007/s00449-007-0128-x

DO - 10.1007/s00449-007-0128-x

M3 - Article

C2 - 17497303

AN - SCOPUS:35748957517

SN - 1615-7591

VL - 30

SP - 327

EP - 330

JO - Bioprocess and Biosystems Engineering

JF - Bioprocess and Biosystems Engineering

IS - 5

ER -

Lipase catalyse glycerolysis for kinetic resolution of racemates

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this