Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free

Candida antarctica lipase B (CALB) is an enzyme able to catalyze chemical reaction, however when it is used as a free enzyme, it cannot be recovered from reaction medium. One of the alternatives is to immobilize the enzymes on a support which allows the maintenance of their catalytic activities. The...

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Bibliographic Details
Published in:Química Nova
Main Authors: Catia S. Z. Battiston, Aline M. M. Ficanha, Katarine L. D. Levandoski, Bernardo A. da Silva, Suellen Battiston, Rogério M. Dallago, Marcelo L. Mignoni
Format: Article in Journal/Newspaper
Language:English
Spanish
Portuguese
Published: Sociedade Brasileira de Química
Subjects:
lipase
immobilization
MCM-48
ionic solid
Chemistry
QD1-999
Antarc*
Antarctica
Online Access:https://doi.org/10.21577/0100-4042.20170011
https://doaj.org/article/96b60a707ce34308a4c7cfc54430f3c0
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Summary:Candida antarctica lipase B (CALB) is an enzyme able to catalyze chemical reaction, however when it is used as a free enzyme, it cannot be recovered from reaction medium. One of the alternatives is to immobilize the enzymes on a support which allows the maintenance of their catalytic activities. The purpose of this paper was to immobilize the CALB on MCM-48 using the ionic solid [C16MI]Cl as structure director. 22 CCRD (Central Composite Rotational Design) was proposed to analyze the influence of the variables like enzyme mass (0.059 to 0.341 g) and ionic solid concentration (0.59 to 3.41%) in the enzyme immobilization process to obtain the maximum esterification activity in order to optimize the process. After immobilization, the study results showed that the enzymes exhibited improvement of thermal (40, 60 and 80 ºC) and storage stability (90 days), besides the possibility to reuse of the enzyme up to 10 times, showing residual activity of 50%.

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