Partial purification of Nigella sativa L. seed lipase and its application in transesterification reactions

Melek Tuter; Francesco Secundo; Sergio Riva; H. Ayşe Aksoy; Guldem Ustun

doi:10.1007/s11746-003-0648-6

Partial purification of Nigella sativa L. seed lipase and its application in transesterification reactions

Melek Tuter, Francesco Secundo, Sergio Riva, H. Ayşe Aksoy^*, Guldem Ustun

^*Corresponding author for this work

Department of Chemical Engineering

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

25 Citations (Scopus)

Abstract

Nigella sativa L. seed lipase isolated from defatted seeds was partially purified and used as catalyst in transesterification reactions. Purification of an ammonium sulfate-precipitated sample (at 35% saturation, Nigella PL) by DEAE ion-exchange chromatography increased the specific activity from 13.9 to 156.7 U/mg protein. Nigella PL and Nigella CPL (the partially purified enzyme sample obtained by DEAE ion-exchange chromatography) catalyzed the transesterification of vinyl acetate with octanol, with racemic sulcatol (6-methyl-5-hepten-2-ol), and with racemic trans-sobrerol (trans-p-menth-6-ene-2,8-diol) in different organic solvents. Both activity and enantioselectivity of the enzyme samples used for these biotransformations were affected by the nature of the organic solvent.

Original language	English
Pages (from-to)	43-48
Number of pages	6
Journal	JAOCS, Journal of the American Oil Chemists' Society
Volume	80
Issue number	1
DOIs	https://doi.org/10.1007/s11746-003-0648-6
Publication status	Published - Jan 2003

Keywords

Enantioselectivity
Enzymatic transesterification
Nigella sativa L. seed lipase
Purification
Sobrerol
Sulcatol

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title = "Partial purification of Nigella sativa L. seed lipase and its application in transesterification reactions",

abstract = "Nigella sativa L. seed lipase isolated from defatted seeds was partially purified and used as catalyst in transesterification reactions. Purification of an ammonium sulfate-precipitated sample (at 35% saturation, Nigella PL) by DEAE ion-exchange chromatography increased the specific activity from 13.9 to 156.7 U/mg protein. Nigella PL and Nigella CPL (the partially purified enzyme sample obtained by DEAE ion-exchange chromatography) catalyzed the transesterification of vinyl acetate with octanol, with racemic sulcatol (6-methyl-5-hepten-2-ol), and with racemic trans-sobrerol (trans-p-menth-6-ene-2,8-diol) in different organic solvents. Both activity and enantioselectivity of the enzyme samples used for these biotransformations were affected by the nature of the organic solvent.",

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author = "Melek Tuter and Francesco Secundo and Sergio Riva and {Ay{\c s}e Aksoy}, H. and Guldem Ustun",

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AU - Secundo, Francesco

AU - Riva, Sergio

AU - Ayşe Aksoy, H.

AU - Ustun, Guldem

PY - 2003/1

Y1 - 2003/1

N2 - Nigella sativa L. seed lipase isolated from defatted seeds was partially purified and used as catalyst in transesterification reactions. Purification of an ammonium sulfate-precipitated sample (at 35% saturation, Nigella PL) by DEAE ion-exchange chromatography increased the specific activity from 13.9 to 156.7 U/mg protein. Nigella PL and Nigella CPL (the partially purified enzyme sample obtained by DEAE ion-exchange chromatography) catalyzed the transesterification of vinyl acetate with octanol, with racemic sulcatol (6-methyl-5-hepten-2-ol), and with racemic trans-sobrerol (trans-p-menth-6-ene-2,8-diol) in different organic solvents. Both activity and enantioselectivity of the enzyme samples used for these biotransformations were affected by the nature of the organic solvent.

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KW - Enzymatic transesterification

KW - Nigella sativa L. seed lipase

KW - Purification

KW - Sobrerol

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Partial purification of Nigella sativa L. seed lipase and its application in transesterification reactions

Abstract

Keywords

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