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

2018; Multidisciplinary Digital Publishing Institute; Volume: 8; Issue: 2 Linguagem: Inglês

10.3390/catal8020084

ISSN

2073-4344

Autores

Fernanda Dell Antonio Facchini, Marita Gimenez Pereira, Ana Cláudia Vici, Marco Filice, Benevides C. Pessela, José M. Guisán, Gloria Fernández‐Lorente, Maria de Lourdes Teixeira de Moraes Polizeli,

Tópico(s)

Electrochemical sensors and biosensors

Resumo

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.

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