Lipase-catalyzed incorporation of conjugated linoleic acid into tricaprylin

In-Hwan Kim, Chil Surk Yoon, Soo H. Cho, Kwang Won Lee, Soo Hyun Chung, Beom Seok Tae

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Three commercially available immobilized lipases, Novozym 435 from Candida antarctica, Lipozyme IM from Rhizomucor miehei, and Lipase PS-C from Pseudomonas cepacia, were used as biocatalysts for the interesterification of conjugated linoleic acid (CLA) ethyl ester and tricaprylin. The reactions were carried out in hexane, and the products were analyzed by gas-liquid chromatography. The effects of molar ratio, enzyme load, incubation time, and temperature on CLA incorporation were investigated. Novozym 435, as compared to Lipozyme IM and Lipase PC-C, showed the highest degree of CLA incorporation into tricaprylin. By hydrolysis with pancreatic lipase, it was found that Lipozyme IM and Lipase PS-C exhibited high selectivity for the sn-1,3 position of the triacylglycerol early in the interesterification, with small extents of incorporation of CLA into the sn-2 position, probably due to acyl migration, at later reaction times. A small extent of sn-1,3 selectivity during interesterification by Novozym 435 was observed.

Original languageEnglish
Pages (from-to)547-551
Number of pages5
JournalJAOCS, Journal of the American Oil Chemists' Society
Volume78
Issue number5
Publication statusPublished - 2001 May 1

Fingerprint

Linoleic acid
Conjugated Linoleic Acids
Lipases
conjugated linoleic acid
Lipase
Pseudozyma antarctica
Rhizomucor miehei
Burkholderia cepacia
Rhizomucor
Biocatalysts
hexane
Candida
triacylglycerol lipase
Liquid chromatography
Hexanes
Enzymes
Hexane
gas chromatography
hydrolysis
Gas chromatography

Keywords

  • Acyl migration
  • Conjugated linoleic acid
  • Immobilized lipase
  • Interesterification
  • Tricaprylin

ASJC Scopus subject areas

  • Food Science
  • Chemistry (miscellaneous)

Cite this

Lipase-catalyzed incorporation of conjugated linoleic acid into tricaprylin. / Kim, In-Hwan; Yoon, Chil Surk; Cho, Soo H.; Lee, Kwang Won; Chung, Soo Hyun; Tae, Beom Seok.

In: JAOCS, Journal of the American Oil Chemists' Society, Vol. 78, No. 5, 01.05.2001, p. 547-551.

Research output: Contribution to journalArticle

Kim, In-Hwan ; Yoon, Chil Surk ; Cho, Soo H. ; Lee, Kwang Won ; Chung, Soo Hyun ; Tae, Beom Seok. / Lipase-catalyzed incorporation of conjugated linoleic acid into tricaprylin. In: JAOCS, Journal of the American Oil Chemists' Society. 2001 ; Vol. 78, No. 5. pp. 547-551.
@article{747b65b359e5409faaaefae99ba1c789,
title = "Lipase-catalyzed incorporation of conjugated linoleic acid into tricaprylin",
abstract = "Three commercially available immobilized lipases, Novozym 435 from Candida antarctica, Lipozyme IM from Rhizomucor miehei, and Lipase PS-C from Pseudomonas cepacia, were used as biocatalysts for the interesterification of conjugated linoleic acid (CLA) ethyl ester and tricaprylin. The reactions were carried out in hexane, and the products were analyzed by gas-liquid chromatography. The effects of molar ratio, enzyme load, incubation time, and temperature on CLA incorporation were investigated. Novozym 435, as compared to Lipozyme IM and Lipase PC-C, showed the highest degree of CLA incorporation into tricaprylin. By hydrolysis with pancreatic lipase, it was found that Lipozyme IM and Lipase PS-C exhibited high selectivity for the sn-1,3 position of the triacylglycerol early in the interesterification, with small extents of incorporation of CLA into the sn-2 position, probably due to acyl migration, at later reaction times. A small extent of sn-1,3 selectivity during interesterification by Novozym 435 was observed.",
keywords = "Acyl migration, Conjugated linoleic acid, Immobilized lipase, Interesterification, Tricaprylin",
author = "In-Hwan Kim and Yoon, {Chil Surk} and Cho, {Soo H.} and Lee, {Kwang Won} and Chung, {Soo Hyun} and Tae, {Beom Seok}",
year = "2001",
month = "5",
day = "1",
language = "English",
volume = "78",
pages = "547--551",
journal = "Oil & Soap",
issn = "0003-021X",
publisher = "Springer Verlag",
number = "5",

}

TY - JOUR

T1 - Lipase-catalyzed incorporation of conjugated linoleic acid into tricaprylin

AU - Kim, In-Hwan

AU - Yoon, Chil Surk

AU - Cho, Soo H.

AU - Lee, Kwang Won

AU - Chung, Soo Hyun

AU - Tae, Beom Seok

PY - 2001/5/1

Y1 - 2001/5/1

N2 - Three commercially available immobilized lipases, Novozym 435 from Candida antarctica, Lipozyme IM from Rhizomucor miehei, and Lipase PS-C from Pseudomonas cepacia, were used as biocatalysts for the interesterification of conjugated linoleic acid (CLA) ethyl ester and tricaprylin. The reactions were carried out in hexane, and the products were analyzed by gas-liquid chromatography. The effects of molar ratio, enzyme load, incubation time, and temperature on CLA incorporation were investigated. Novozym 435, as compared to Lipozyme IM and Lipase PC-C, showed the highest degree of CLA incorporation into tricaprylin. By hydrolysis with pancreatic lipase, it was found that Lipozyme IM and Lipase PS-C exhibited high selectivity for the sn-1,3 position of the triacylglycerol early in the interesterification, with small extents of incorporation of CLA into the sn-2 position, probably due to acyl migration, at later reaction times. A small extent of sn-1,3 selectivity during interesterification by Novozym 435 was observed.

AB - Three commercially available immobilized lipases, Novozym 435 from Candida antarctica, Lipozyme IM from Rhizomucor miehei, and Lipase PS-C from Pseudomonas cepacia, were used as biocatalysts for the interesterification of conjugated linoleic acid (CLA) ethyl ester and tricaprylin. The reactions were carried out in hexane, and the products were analyzed by gas-liquid chromatography. The effects of molar ratio, enzyme load, incubation time, and temperature on CLA incorporation were investigated. Novozym 435, as compared to Lipozyme IM and Lipase PC-C, showed the highest degree of CLA incorporation into tricaprylin. By hydrolysis with pancreatic lipase, it was found that Lipozyme IM and Lipase PS-C exhibited high selectivity for the sn-1,3 position of the triacylglycerol early in the interesterification, with small extents of incorporation of CLA into the sn-2 position, probably due to acyl migration, at later reaction times. A small extent of sn-1,3 selectivity during interesterification by Novozym 435 was observed.

KW - Acyl migration

KW - Conjugated linoleic acid

KW - Immobilized lipase

KW - Interesterification

KW - Tricaprylin

UR - http://www.scopus.com/inward/record.url?scp=0035328932&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035328932&partnerID=8YFLogxK

M3 - Article

VL - 78

SP - 547

EP - 551

JO - Oil & Soap

JF - Oil & Soap

SN - 0003-021X

IS - 5

ER -