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

Araştırma sonucu: ???type-name???Makalebilirkişi

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 dilİngilizce
Sayfa (başlangıç-bitiş)43-48
Sayfa sayısı6
DergiJAOCS, Journal of the American Oil Chemists' Society
Hacim80
Basın numarası1
DOI'lar
Yayın durumuYayınlandı - 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.

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

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