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RevistaProcess Biochemistry
Año2019
Volumen87
Páginas128-137
Internacional

Modulation of Lecitase properties via immobilization on differently activated Immobead-350: stabilization and inversion of enantiospecificity

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Maísa P. Pinheiroa, Rodolpho R. C. Monteiroa, Francisco F. M. Silvab, Telma L. G. Lemosc, Roberto Fernandez-Lafuented*, Luciana R. B. Gonçalvesa* and José C. S. dos Santose*.
a Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455-760, Fortaleza, CE, Brazil.
b Instituto Federal de Educação, Ciência e Tecnologia do Rio Grande do Norte, RN 233, Km-02, Nº 999, Bairro Chapada do Apodi, Apodi CEP 59700-000, Rio Grande do Norte, Brazil.
c Departamento de Química Orgânica e Inorgânica da Universidade Federal do Ceará, Campus do Pici, Bloco 940, Fortaleza CEP 60455-760, Ceará, Brazil
d Departamento de Biocatálisis, Instituto de Catálisis-CSIC, C/Marie Curie 2, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain.
e Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, CEP.: 62.790-970, Redenção, CE, Brazil.
 
 
Lecitase Ultra (Leci) was immobilized on Immobead-350 (IB-350) activated with epoxy (EPO), amino-divinylsulfone (DVS) or amino-glutaraldehyde (GLU) groups. Leci-GLU had 27% more activity versus p-nitro-phenyl butyrate (p-NPB) than Leci-EPO, after 3 hours of immobilization using 100 mg of enzyme/g of support (immobilization yield was 84.1%, expressed activity versus p-NPB  was around 10%), the covalent immobilization was show for Leci-GLU and Leci-DVS . After 10 consecutive cycles of p-NPB hydrolysis, its activity remained unaltered. Leci-GLU was the most stable preparation at 65 °C and pH 7 (29 folds more stable than the free enzyme) and in the presence of 30% acetonitrile at 30 ºC and pH 7 (almost 2 folds more stable than the free enzyme). Very interestingly, the activity versus methyl mandelate and synthesis of benzyl acetate was quite high. Although the other biocatalysts had preference for the S-methyl mandelate, Leci-GLU preferred the R-isomer at pHs 5 (VR/VS = 6.6) and 7 (VR/VS = 3.5). In the enzymatic synthesis of benzyl acetate, the most active biocatalyst was also Leci-GLU (2.1 U/mg), being almost 2 folds more active than Leci-DVS. According to the results, it was concluded that the Lecitase immobilization on IB-350 using different chemistries greatly influenced its catalytic properties.
 
Palabras clave:glutaraldehyde, divinylsulfone, biocatalysts immobilization, Lecitase stabilization, modulation of Lecitase, epoxide.
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