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Article

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

1
Departamento de Medicina, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, 14040-900 Sao Paulo, Brazil
2
Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, 14040-901 Sao Paulo, Brazil
3
Nanobiotechnology, Molecular Imaging and Metabolomics Group, Spanish National Centre for Cardiovascular Research–CNIC, 28029 Madrid, Spain
4
Departamento de Biotecnología y Microbiologia de los Alimentos, Instituto de Ciencias de la Alimentación, CIAL-CSIC, Calle Nicolás Cabrera 9, CampusUAM, 28049 Cantoblanco, Spain
5
Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica—CSIC, Campus UAM, Cantoblanco, 28049 Madrid, Spain
*
Author to whom correspondence should be addressed.
Catalysts 2018, 8(2), 84; https://doi.org/10.3390/catal8020084
Received: 15 December 2017 / Revised: 30 January 2018 / Accepted: 2 February 2018 / Published: 16 February 2018
(This article belongs to the Special Issue Immobilized Biocatalysts)
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. View Full-Text
Keywords: immobilization; purification; lipase; Fusarium verticillioides; EPA; DHA immobilization; purification; lipase; Fusarium verticillioides; EPA; DHA
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MDPI and ACS Style

Facchini, F.D.A.; Pereira, M.G.; Vici, A.C.; Filice, M.; Pessela, B.C.; Guisan, J.M.; Fernandez-Lorente, G.; Polizeli, M.D.L.T.d.M. Immobilization Effects on the Catalytic Properties of Two Fusarium Verticillioides Lipases: Stability, Hydrolysis, Transesterification and Enantioselectivity Improvement. Catalysts 2018, 8, 84. https://doi.org/10.3390/catal8020084

AMA Style

Facchini FDA, Pereira MG, Vici AC, Filice M, Pessela BC, Guisan JM, Fernandez-Lorente G, Polizeli MDLTdM. Immobilization Effects on the Catalytic Properties of Two Fusarium Verticillioides Lipases: Stability, Hydrolysis, Transesterification and Enantioselectivity Improvement. Catalysts. 2018; 8(2):84. https://doi.org/10.3390/catal8020084

Chicago/Turabian Style

Facchini, Fernanda D.A., Marita G. Pereira, Ana C. Vici, Marco Filice, Benevides C. Pessela, Jose M. Guisan, Glória Fernandez-Lorente, and Maria D.L.T.d.M. Polizeli 2018. "Immobilization Effects on the Catalytic Properties of Two Fusarium Verticillioides Lipases: Stability, Hydrolysis, Transesterification and Enantioselectivity Improvement" Catalysts 8, no. 2: 84. https://doi.org/10.3390/catal8020084

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