Activity and adsorption of lipase from Nigella sativa seeds on Celite at different pH values

Akova A., Ustun G.

BIOTECHNOLOGY LETTERS, vol.22, no.5, pp.355-359, 2000 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 22 Issue: 5
  • Publication Date: 2000
  • Doi Number: 10.1023/a:1005668500716
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.355-359
  • Istanbul Technical University Affiliated: No


Lipase from Nigella sativa seeds was immobilized by adsorption on Celite 535 from phosphate buffer solutions varying pH values of 5.0-8.0 at 25 degrees C. Langmuir isotherms described the adsorption equilibria well for lipase adsorption at all pH range. The saturation capacity for adsorption of lipase increased from 14.5 to 24.3 mg g(-1) Celite as the adsorption pH was reduced from 8 to 5, but the adsorption equilibrium constant remained constant and was determined to be 1.92 x 10(5) M-1. The adsorbed enzymes showed different activity values depending on the pH of the adsorption medium. The immobilized enzymes prepared at pH 6 displayed the highest activity values.