Advanced search
Start date
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

Full text
Antonio Facchini, Fernanda Dell [1] ; Pereira, Marita Gimenez [2] ; Vici, Ana Claudia [2] ; Filice, Marco [3] ; Costa Pessela, Benevides [4] ; Manuel Guisan, Jose [5] ; Fernandez-Lorente, Gloria [4] ; Teixeira de Moraes Polizeli, Maria de Lourdes [2]
Total Authors: 8
[1] Univ Sao Paulo, Dept Med, Fac Med Ribeirao Preto, BR-14040900 Sao Paulo - Brazil
[2] Univ Sao Paulo, Dept Biol, Fac Filosofia Ciencias & Letras Ribeirao Preto, BR-14040901 Sao Paulo - Brazil
[3] Spanish Natl Ctr Cardiovasc Res, CNIC, Nanobiotechnol Mol Imaging & Metabol Grp, Madrid 28029 - Spain
[4] CSIC, CIAL, Inst Ciencias Alimentac, Dept Biotecnol & Microbiol Alimentos, Calle Nicolas Cabrera 9, CampusUAM, Canto Blanco 28049 - Spain
[5] CSIC, Inst Catalisis & Petroleoquim, Dept Biocatalisis, Campus UAM, Canto Blanco 28049 - Spain
Total Affiliations: 5
Document type: Journal article
Source: CATALYSTS; v. 8, n. 2 FEB 2018.
Web of Science Citations: 4

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 degrees C. They were thermostable at 40 degrees 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. (AU)

FAPESP's process: 13/50892-5 - Development of strategies of immobilization and use of enzymes as biocatalysis for industrial applications: production of biodiesel and functional ingredients
Grantee:Maria de Lourdes Teixeira de Moraes Polizeli
Support type: Regular Research Grants