Kinetic study of the lipase-catalyzed interesterification of triolein and stearic acid in nonpolar media

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The kinetics of the interesterification of triolein and stearic acid catalyzed by immobilized Rhizopus delemar lipase were studied in a batch operation. In order to clarify the mechanisms of this reaction, three models are discussed under various conditions in terms of the ratio of triolein and stearic acid. The rate constants involved in the proposed model were determined by combining the numerical Gauss-elemination method, and the trial-and-error method so as to fit the calculated results with the experimental data. The accuracy of the obtained rate constants was confirmed after they were substituted for simultaneous differential equations and the equations simulated using an adaptive step-size Runge-Kutta method. Finally, the model which agrees with the calculated results and the experimental data was selected.

Original languageEnglish
Pages (from-to)7-12
Number of pages6
JournalJournal of Biochemistry and Molecular Biology
Volume30
Issue number1
Publication statusPublished - 1997 Jan 31

Keywords

  • 1,3-specific lipase
  • Kinetics
  • Modeling
  • Rate constants
  • Simulation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Kinetic study of the lipase-catalyzed interesterification of triolein and stearic acid in nonpolar media'. Together they form a unique fingerprint.

  • Cite this