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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.)

Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts

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Author(s):
Mendes, Adriano A. [1, 2] ; de Castro, Heizir F. [3] ; Rodrigues, Dasciana de S. [1] ; Adriano, Wellington S. [1] ; Tardioli, Paulo W. [1] ; Mammarella, Enrique J. [4] ; Giordano, Roberto de C. [1] ; Giordano, Raquel de L. C. [1]
Total Authors: 8
Affiliation:
[1] Univ Fed Sao Carlos, Dept Chem Engn, BR-13565905 Sao Carlos, SP - Brazil
[2] Univ Fed Sao Joao del Rei, BR-37501970 Sete Lagoas, MG - Brazil
[3] Univ Sao Paulo, Dept Chem Engn, Engn Sch Lorena, BR-12602810 Lorena, SP - Brazil
[4] Natl Univ Litoral, Inst Technol Dev Chem Ind, Santa Fe, NM - USA
Total Affiliations: 4
Document type: Journal article
Source: Journal of Industrial Microbiology & Biotechnology; v. 38, n. 8, p. 1055-1066, AUG 2011.
Web of Science Citations: 55
Abstract

This work aimed at the production of stabilized derivatives of Thermomyces lanuginosus lipase (TLL) by multipoint covalent immobilization of the enzyme on chitosan-based matrices. The resulting biocatalysts were tested for synthesis of biodiesel by ethanolysis of palm oil. Different hydrogels were prepared: chitosan alone and in polyelectrolyte complexes (PEC) with kappa-carrageenan, gelatin, alginate, and polyvinyl alcohol (PVA). The obtained supports were chemically modified with 2,4,6-trinitrobenzene sulfonic acid (TNBS) to increase support hydrophobicity, followed by activation with different agents such as glycidol (GLY), epichlorohydrin (EPI), and glutaraldehyde (GLU). The chitosan-alginate hydrogel, chemically modified with TNBS, provided derivatives with higher apparent hydrolytic activity (HA(app)) and thermal stability, being up to 45-fold more stable than soluble lipase. The maximum load of immobilized enzyme was 17.5 mg g(-1) of gel for GLU, 7.76 mg g(-1) of gel for GLY, and 7.65 mg g(-1) of gel for EPI derivatives, the latter presenting the maximum apparent hydrolytic activity (364.8 IU g(-1) of gel). The three derivatives catalyzed conversion of palm oil to biodiesel, but chitosan-alginate-TNBS activated via GLY and EPI led to higher recovered activities of the enzyme. Thus, this is a more attractive option for both hydrolysis and transesterification of vegetable oils using immobilized TLL, although industrial application of this biocatalyst still demands further improvements in its half-life to make the enzymatic process economically attractive. (AU)