IMMOBILIZATION OF LIPASE ON MESOPOROUS MOLECULAR SIEVE MCM-48 OBTAINED USING IONIC SOLID AS A STRUCTURE DIRECTOR AND ESTERIFICATION REACTION ON SOLVENT-FREE

被引：7

作者：

Battiston, Catia S. Z. ^{[1
]}

Ficanha, Aline M. M. ^{[2
]}

Levandoski, Katarine L. D. ^{[2
]}

da Silva, Bernardo A. ^{[2
]}

Battiston, Suellen ^{[3
]}

Dallago, Rogerio M. ^{[2
]}

Mignoni, Marcelo L. ^{[2
]}

机构：

[1] Inst Fed Rio Grande do Sul, BR-99971302 Erechim, RS, Brazil

[2] Univ Reg Integrada Alto Uruguai & Missoes, Dept Quim, BR-99709910 Erechim, RS, Brazil

[3] Univ Fed Santa Catarina, Dept Engn Quim, BR-88040970 Florianopolis, SC, Brazil

来源：

QUIMICA NOVA | 2017年 / 40卷 / 03期

关键词：

lipase; immobilization; MCM-48; ionic solid; SILICA; SURFACTANT;

D O I：

10.21577/0100-4042.20170011

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. 2(2) 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 degrees C) and storage stability (90 days), besides the possibility to reuse of the enzyme up to 10 times, showing residual activity of 50%.

引用

页码：293 / 298

页数：6

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