IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS

AUTOR(ES)

Carneiro, Elizabete Araújo; Bastos, Ana Karine Pessoa; Oliveira, Ulisses Marcondes Freire de; Matos, Leonardo José Brandão Lima de; Adriano, Wellington Sabino; Monteiro, Rodolpho Ramilton de Castro; Santos, José Cleiton Sousa dos; Gonçalves, Luciana Rocha Barros

FONTE

Quím. Nova

DATA DE PUBLICAÇÃO

2020-09

RESUMO

The lipase from Rhizomucor miehei (RML) has been immobilized on chitosan-based hybrid (sodium alginate or carrageenan) matrices activated with glycidol (GLY), epichlorohydrin (EPI) or glutaraldehyde (GLU) groups. Then, the properties of the different biocatalysts have been evaluated and compared with the soluble RML. Thermal stability (at pH 7.0 and 60 °C) was significantly increased when compared to the soluble enzyme: 154-fold for chitosan 5.0% - GLU, 80-fold for chitosan 2.5% - carrageenan 2.5% - GLY and 93-fold for chitosan 2.5% - alginate 2.5% - EPI. The best biocatalyst preparation, which was 154-fold more stable than the soluble enzyme, was obtained when RML was immobilized on chitosan activated with glutaraldehyde 5.0% v/v. According to the results, it was concluded that RML immobilization on chitosan-based hybrid matrices using different chemistries greatly produced biocatalysts with different properties.

Documentos Relacionados

• Stability of immobilized Rhizomucor miehei lipase for the synthesis of pentyl octanoate in a continuous packed bed bioreactor
• Theoretical investigation of the dynamics of the active site lid in Rhizomucor miehei lipase.
• LIPASE - CATALYZED FORMATION OF PENTYL NONANOATE USING SCREENED IMMOBILIZED LIPASE FROM Rhizomucor meihei
• Glicerólise de óleo de peixe catalisada por lipase comercial de Rhizomucor miehei em meio com surfactante de grau alimentício
• Immobilization and catalytic properties of lipase on chitosan for hydrolysis and esterification reactions