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


Tuter M. , SECUNDO F., RIVA S., AKSOY H., USTUN G.

JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, cilt.80, ss.43-48, 2003 (SCI İndekslerine Giren Dergi) identifier identifier

  • Cilt numarası: 80 Konu: 1
  • Basım Tarihi: 2003
  • Doi Numarası: 10.1007/s11746-003-0648-6
  • Dergi Adı: JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
  • Sayfa Sayıları: ss.43-48

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.