The hydrolysis of corn oil in the presence of a lipase from Pseudomonas sp. immobilized within the walls of a hollow-fiber reactor was studied at 30ยฐC. To assess the selectivity of this immobilized enzyme, the effluent concentrations of five different free fatty acids were measured using high-perfor
Biotechnology for the production of nutraceuticals enriched in conjugated linoleic acid: I. Uniresponse kinetics of the hydrolysis of corn oil by a Pseudomonas sp. lipase immobilized in a hollow fiber reactor
โ Scribed by Prima S. Sehanputri; Charles G. Hill Jr.
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 227 KB
- Volume
- 64
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
โฆ Synopsis
The kinetics of the hydrolysis of corn oil in the presence of a lipase from Pseudomonas sp. immobilized within the walls of a hollow fiber reactor can be modeled in terms of a three-parameter rate expression. This rate expression consists of the product of a two-parameter rate expression for the hydrolysis reaction itself (which is of the general Michaelis-Menten form) and a first-order rate expression for deactivation of the enzyme.
Optimum operating conditions correspond to 30ยฐC and buffer pH values of 7.0 during both immobilization of the enzyme and the hydrolysis reaction. Under these conditions, the total fatty acid concentration in the effluent oil stream for a fluid residence time of 4 h is approximately 1.6 M. This concentration corresponds to hydrolysis of approximately 50% of the glyceride bonds present in the feedstock corn oil. The fatty acid of primary interest in the effluent stream is linoleic acid.
๐ SIMILAR VOLUMES
A calf pregastric esterase immobilized in a hollow-fiber reactor was employed to hydrolyze milkfat, thereby producing a lipolyzed butteroil. The reaction kinetics can be modeled by a two-parameter model of the general Michaelis-Menten form based on a ping-pong bi-bi mechanism; the rate of enzyme dea