Hypocrea pseudokoningii purified lipase was immobilized on hydrophobic supports (phenyl-sepharose, butyl-sepharose, octyl-sepharose, Hexyl Toyopearl, Lewatit, Purolite, Decaoctyl sepabeads) and ionic supports (Duolite, DEAE-agarose, PEI-agarose, MANAE-agarose, and Q-sepharose). The immobilization processes resulted in derivatives with excellent thermal stabilities, increasing the half-life up to 500-fold. The derivatives had excellent stability to organic solvents compared to the crude lipase. In the presence of 50% ethanol, hexyl and Decaoctyl derivatives increased by about 6- and 3.5-fold their stability to organic solvents, respectively. When tested for methanol, phenyl-sepharose derivative also increased their stability to organic solvents in approximately 2-fold. Octyl-sepharose derivative was fully stable for 48 h in the presence of propanol, which showed a half-life of about 7.5 h. The greater activation of the derivatives occurred using 50% cyclohexane, in which the hexyl derivative obtained an increase in the activity of 9-fold and phenyl and octyl derivatives had their activity increased by 6-fold. The lipase showed activity on different oils. Therefore, the adsorption of lipases in low ionic strength and highly hydrophobic supports is shown to be a simple and rapid tool for the immobilization of H. pseudokoningii lipase. These derivatives strongly increase the chances of this biocatalyst for industrial application.

This work was supported by grants from Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP), Conselho de Desenvolvimento Científico e Tecnológico (CNPq process n° 406838/2013-5). This project is also part of National Institute of Science and Technology of the Bioethanol (n° 574002/2008-1), CNPq – Ciência sem Fronteira (n° 242775/2012-8). JAJ and MLTMP are Research Fellows of CNPq. MGP and ACV are supported by CNPq. FDAF was recipient FAPESP Fellowship.

Peer Reviewed