•Immobilised Candida antarctica lipase B (CAL-B) and support material (immobead-150) were characterised.
Non-selective hydrolysis of tuna fish oil for producing free fatty acids containing docosahexaenoic acid
Article first published online: 29 MAY 2013
Copyright © 2013 Canadian Society for Chemical Engineering
The Canadian Journal of Chemical Engineering
Volume 92, Issue 2, pages 344–354, February 2014
How to Cite
Sharma, A., Chaurasia, S. P. and Dalai, A. K. (2014), Non-selective hydrolysis of tuna fish oil for producing free fatty acids containing docosahexaenoic acid. Can. J. Chem. Eng., 92: 344–354. doi: 10.1002/cjce.21851
•The Michaelis–Menten kinetic model and activation energy were studied for hydrolysis.
•Activity of CAL-B was studied up to five runs of repeated use.
•Tuna fish oil was effectively hydrolysed with CAL-B to produce DHA-rich free fatty acids.
- Issue published online: 19 JAN 2014
- Article first published online: 29 MAY 2013
- Manuscript Revised: 8 JAN 2013
- Manuscript Accepted: 8 JAN 2013
- Manuscript Received: 4 AUG 2012
- University of Saskatchewan Graduate Student Exchange Program
- polyunsaturated fatty acids;
- immobilised CAL-B;
- kinetic study
The nature of immobilised Candida antarctica lipase-B (CAL-B) catalysed hydrolysis of tuna fish oil was studied with parameters such as solvent and water concentration, temperature, speed of agitation and enzyme loading. Immobilised CAL-B and support material immobead-150 were characterised with BET surface area, particle size analyser and Fourier transform infrared spectroscopy (FT-IR) to record their physiochemical properties. The maximum rate of reaction (Vmax) of 500 µmol of free fatty acids (FFAs) per mL reaction mixture per h and Michaelis−Menten constant (KM) of 2115 µmol FFAs/mL were found for Michaelis−Menten type kinetic model. Activation energy (E) of 26.1 KJ/mol was calculated for immobilised CAL-B. The 55.9% conversion of triglycerides was observed after the third use of the immobilised CAL-B. The activity retention of immobilised CAL-B reduced to 33.5% after the fourth repeated use of the enzyme.