Immobilization Effects on the Catalytic Properties of Two Fusarium Verticillioides Lipases: Stability, Hydrolysis, Transesterification and Enantioselectivity Improvement

Author： Facchini Fernanda Dell Antonio Pereira Marita Gimenez Vici Ana Claudia Filice Marco Pessela Benevides Costa Guisan Jose Manuel Fernandez-Lorente Glória Polizeli Maria de Lourdes Teixeira de Moraes

Publisher： MDPI

E-ISSN： 2073-4344|8|2|84-84

ISSN： 2073-4344

Source： Catalysts, Vol.8, Iss.2, 2018-02, pp. : 84-84

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Abstract

Fusarium verticillioides lipases were purified in a “cascade” method using octadecyl Sepabeads and octyl Sepharose resins, which led to the isolation of two proteins with lipolytic activities. Lip 1 was purified after octyl Sepharose adsorption presenting 30.3 kDa and, Lip 2 presented 68.0 kDa after octadecyl adsorption. These immobilization processes resulted in an increase of 3-fold in activity of each immobilized enzyme. These enzymes presented optima of pH of 5.0 and 6.0, respectively and temperature at 40 °C. They were thermostable at 40 °C and both remained more than 50% of its activity at the pH range of 5.0 to 7.0, with 180 min of incubation. The sardine oil hydrolysis showed higher EPA/DHA ratio. Concerning the ethanolysis reaction, Lip 2 showed higher conversion (5.5%) and both lipases showed activity in the release of the S enantiomers from 2-O-butyryl-2-phenylacetic acid (mandelic butyrate acid) and HPBE hydrolysis. Lip 2 also demonstrated capacity of transesterification. These applications made these enzymes attractive for industrial application.