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

Autor(es)

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]

Afiliação do(s) autor(es)

^[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

• Tipo de documento: Artigo Científico
• Fonte: Journal of Industrial Microbiology & Biotechnology; v. 38, n. 8, p. 1055-1066, AUG 2011.
• Citações Web of Science: 55

Resumo

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)

• Processo FAPESP: 04/14593-4 - Síntese de biodiesel por interesterificação enzimática de óleos vegetais empregando lipase estabilizada pela técnica multipontual
• Beneficiário: Adriano Aguiar Mendes
• Modalidade de apoio: Bolsas no Brasil - Doutorado