16
Views
10
CrossRef citations to date
0
Altmetric
Research Article

Application of encapsulated enzyme as a continuous packed-bed reactor

, , , &
Pages 285-299 | Received 24 May 1988, Accepted 16 Jun 1988, Published online: 27 Sep 2008
 

Abstract

In the previous report, microencapsulation of lipase employing a (w/o)/w multiple phase emulsion technique, with 2: 1 polystyrene (PS)–SBR mixture being used as a wall material, was proposed. Catalysis of the encapsulated enzyme was investigated, and the hydrolysis of triacetin (triglyceride of acetic acid) was successfully simulated by the reaction model based upon the Michaelis-Menten mechanism. Other factors affecting the mechanism such as the mass-transfer resistance of the substrate molecules through the wall and the decrease in pH due to the formation of acetic acid were also taken into consideration.

In this report, the particular microcapsules were applied to the continuous tubular reactor system, essentially a packed column reactor, and longevity and mechanical strength of the microcapsules were fully demonstrated.

The reaction model derived for a well-stirred batch reactor was also applicable to simulate the behaviour in the packed-column reactor as it was proved that there is no mass transfer resistance between the reactant stream and the surface of microcapsules. the observed data agreed quite well with the calculated values. Similarity of the behaviours of catalysis observed between two reactor systems was thoroughly confirmed.

No leakage of the enzyme was detected after repeated usage over the duration of a few months, the temperature being maintained in the range between 293 and 323 K, and pH reset after each operation.

Commercial feasibility of the microcapsules for the enzyme catalysis with substrates, small enough to permeate through the wall, was established by these fundamental investigations.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.