Influence of the use of Aliquat 336 in the immobilization procedure in sol-gel of lipase from Bacillus sp ITP-001
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
21/08/2013
21/08/2013
2012
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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 |
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 |