Influence of the use of Aliquat 336 in the immobilization procedure in sol-gel of lipase from Bacillus sp ITP-001


Autoria(s): Souza, Ranyere L.; Resende, Wagner C.; Barao, Carlos E.; Zanin, Gisella M.; Castro, Heizir F. de; Santos, Onelia A. A.; Fricks, Alini T.; Figueiredo, Renan T.; Lima, Alvaro S.; Soares, Cleide M. F.
Contribuinte(s)

UNIVERSIDADE DE SÃO PAULO

Data(s)

21/08/2013

21/08/2013

2012

Resumo

Aliquat 336, a liquid hydrophobic material, was used at different concentrations (0.5-3.0%, w/v) as an additive in the preparation of encapsulated lipase from Bacillus sp. ITP-001 on sol-gel silica matrices using tetraethoxysilane (TEOS) as the precursor. The resulting hydrophobic matrices and immobilized lipases were characterized with regard to specific surface area (BET method), adsorption-desorption isotherms, pore volume (Vp) and size (dp) by nitrogen adsorption (BJH method) and scanning electron microscopy (SEM). The catalytic activities and the corresponding coupling yields were assayed in the hydrolysis of olive oil. In comparison with pure silica matrices, the immobilization process in the presence of Aliquat 336 decreased the values for specific surface area and increased the values for pore specific volume (Vp) and mean pore diameter (dp). This behavior may be related to the partial adsorption of the enzyme on the external surface of the hydrophobic matrix as indicated by scanning electron microscopy. Aliquat 336 concentrations in the range from 0.5 to 1.5% (w/v) provided immobilized derivatives with higher coupling yields and better substrate affinity. The highest coupling yield (Y-A = 71%) was obtained for the immobilized enzyme prepared in the presence of 1.5% Aliquat which gave the following morphological properties: specific surface area = 183 m(2)/g, pore specific volume (Vp) = 0.36 cc/g and mean pore diameter (dp)= 91 angstrom. (c) 2012 Elsevier B.V. All rights reserved.

Identificador

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, AMSTERDAM, v. 84, n. 3, pp. 152-159, DEC, 2012

1381-1177

http://www.producao.usp.br/handle/BDPI/32662

10.1016/j.molcatb.2012.05.013

http://dx.doi.org/10.1016/j.molcatb.2012.05.013

Idioma(s)

eng

Publicador

ELSEVIER SCIENCE BV

AMSTERDAM

Relação

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC

Direitos

closedAccess

Copyright ELSEVIER SCIENCE BV

Palavras-Chave #LIPASE #IMMOBILIZATION #SOL-GEL #ALIQUAT 336 #PARTICLE-STABILIZED EMULSIONS #COVALENT IMMOBILIZATION #CANDIDA-RUGOSA #IONIC LIQUIDS #SILICA #OIL #ENCAPSULATION #BIOREACTOR #MEMBRANES #SURFACE #BIOCHEMISTRY & MOLECULAR BIOLOGY #CHEMISTRY, PHYSICAL
Tipo

article

original article

publishedVersion