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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Immobilization and stabilization of microbial lipases by multipoint covalent attachment on aldehyde-resin affinity: Application of the biocatalysts in biodiesel synthesis

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Author(s):
Mendes, Adriano A. [1, 2] ; Giordano, Roberto C. [1] ; Giordano, Raquel de L. C. [1] ; de Castro, Heizir F. [3]
Total Authors: 4
Affiliation:
[1] Univ Fed Sao Carlos, Dept Chem Engn, BR-13565905 Sao Carlos, SP - Brazil
[2] Univ Fed Sao Joao del Rei, BR-35701970 Sete Lagoas, MG - Brazil
[3] Univ Sao Paulo, Dept Chem Engn, Engn Sch Lorena, BR-12602810 Lorena, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC; v. 68, n. 1, p. 109-115, JAN 2011.
Web of Science Citations: 64
Abstract

Microbial lipase preparations from Thermomyces lanuginosus (TLL) and Pseudomonas fluorescens (PFL) were immobilized by multipoint covalent attachment on Toyopearl AF-amino-650M resin and the most active and thermal stable derivatives used to catalyze the transesterificanon reaction of babassu and palm oils with ethanol in solvent-free media For this different activating agents mainly glutaraldehyde glycidol and epichlorohydrin were used and immobilization parameters were estimated based on the hydrolysis of olive oil emulsion and butyl butyrate synthesis ILL immobilized on glyoxyl-resin allowed obtaining derivatives with the highest hydrolytic activity (HA(der)) and thermal stability between 27 and 31 times more stable than the soluble lipase Although PFL derivatives were found to be less active and thermally stables similar formation of butyl butyrate concentrations were found for both ILL and PFL derivatives The highest conversion into biodiesel was found in the transesterification of palm oil catalyzed by both ILL and PFL glyoxyl-derivatives (c) 2010 Elsevier B V All rights reserved (AU)