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

^*Bu çalışma için yazışmadan sorumlu yazar

Kimya Mühendisliği Bölümü

Araştırma sonucu: Dergiye katkı › Makale › bilirkişi

25 Atıf (Scopus)

Özet

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.

Orijinal dil	İngilizce
Sayfa (başlangıç-bitiş)	43-48
Sayfa sayısı	6
Dergi	JAOCS, Journal of the American Oil Chemists' Society
Hacim	80
Basın numarası	1
DOI'lar	https://doi.org/10.1007/s11746-003-0648-6
Yayın durumu	Yayınlandı - Oca 2003

Finansman

We are grateful to CNR (Consiglio Nazionale delle Ricerche, Italy) and TUBITAK (Turkish Scientific and Technical Research Center) for financial support of this joint research project. The facilities of the laborotorium of the Chemical Engineering Department, Istanbul Technical University, Turkey are also acknowledged.

Finansörler	Finansör numarası
TUBITAK
Turkish Scientific and Technical Research Center
Consiglio Nazionale delle Ricerche

Belgeye Erişim

10.1007/s11746-003-0648-6

Diğer Dosyalar ve Linkler

Link to publication in Scopus

Alıntı Yap

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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.",

keywords = "Enantioselectivity, Enzymatic transesterification, Nigella sativa L. seed lipase, Purification, Sobrerol, Sulcatol",

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

year = "2003",

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doi = "10.1007/s11746-003-0648-6",

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T1 - Partial purification of Nigella sativa L. seed lipase and its application in transesterification reactions

AU - Tuter, Melek

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.

AB - 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.

KW - Enantioselectivity

KW - Enzymatic transesterification

KW - Nigella sativa L. seed lipase

KW - Purification

KW - Sobrerol

KW - Sulcatol

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M3 - Article

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JF - JAOCS, Journal of the American Oil Chemists' Society

IS - 1

ER -

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

Özet

Finansman

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Diğer Dosyalar ve Linkler

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