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

Autor:	Francesco Secundo, Sergio Riva, Guldem Ustun, H. Ayşe Aksoy, Melek Tüter
Rok vydání:	2003
Předmět:	Octanol Chromatography biology Chemistry General Chemical Engineering Organic Chemistry Nigella sativa Triacylglycerol lipase Transesterification biology.organism_classification Nigella chemistry.chemical_compound biology.protein Vinyl acetate Ammonium Lipase
Zdroj:	Journal of the American Oil Chemists' Society. 80:43-48
ISSN:	0003-021X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::16a3ffb1b9bb4e02ac53c7ad7b9de1fb https://doi.org/10.1007/s11746-003-0648-6 Zobrazit plný text záznamu Full text from SpringerLink Plný text