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RevistaBiotechnology progress
Año2018
Volumen34
Páginas878-889
Internacional

Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead-350

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Maísa Pessoa Pinheiroa, Nathalia Saraiva Riosa, Thiago de S. Fonsecab, Francisco de Aquino
Bezerrab, Enrique Rodríguez-Castellónc, Roberto Fernandez-Lafuented, Marcos Carlos de
Mattosb, José C. S. dos Santose,*, Luciana R. B. Gonçalvesa,*

a Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici,
CEP 60455-760, Fortaleza, CE, Brazil.
b Departamento de Química Orgânica e Inorgânica, Laboratório de Biotecnologia e Síntese
Orgânica (LABS), Universidade Federal do Ceará, Campus do Pici, Caixa Postal 6044,
60455-970 Fortaleza, CE, Brazil.
cDepartamento de Química Inorgánica, Facultad de Ciencias, Universidad de Málaga,
Campus de Teatinos, Boulevard Louis Pasteur, 29010, Málaga, Spain.
d Departamento de biocatalisis. ICP-CSIC. Campus UAM-CSIC. Cantoblanco. 28049 Madrid.
Spain.
eInstituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração
Internacional da Lusofonia Afro-Brasileira, CEP 62785-000, Acarape, CE, Brazil.
 
Novozyme 435, which is a commercial immobilized lipase B from Candida antarctica
(CALB), has been proven to be inadequate for the kinetic resolution of rac-indanyl acetate. As
it has been previously described that different immobilization protocols may greatly alter
lipase features, in this work CALB was covalently immobilized on epoxy Immobead-350 (IB-
350) and on glyoxyl-agarose to ascertain if better kinetic resolution would result. Afterwards,
all CALB biocatalysts were utilized in the hydrolytic resolution of rac-indanyl acetate and
rac-(chloromethyl)-2-(o-methoxyphenoxy)ethyl acetate. After optimization of the
immobilization protocol on IB-350, its loading capacity was 150 mg protein/g dried support.
Furthermore, the CALB-IB-350 thermal and solvent stabilities were higher than that of the
soluble enzyme (e. g., by a 14-fold factor at pH 5 - 70°C and by a 11-fold factor in dioxane
30% - 65°C) and that of the glyoxyl-agarose-CALB (e.g., by a 12-fold factor at pH 10 - 50°C
and by a 21-fold factor in dioxane 30% - 65°C). The CALB-IB-350 preparation (with 98 %
immobilization yield and activity versus p-nitrophenyl butyrate of 6.26 ± 0.2 U/g) was used in
the hydrolysis of rac-indanyl acetate using a biocatalyst/substrate ratio of 2:1 and a pH value
of 7.0 at 30°C for 24 h. The conversion obtained was 48% and the enantiomeric excess of the
product (e.e.p) was 97%. These values were much higher than the ones obtained with
Novozyme 435, 13 % and 26 % of conversion and e.e.p, respectively.

Palabras clave:lipase immobilization–stabilization; epoxy-support; covalent immobilization, rac-indanyl acetate, rac-(chloromethyl)-2-(o-methoxyphenoxy)ethyl acetate; lipase B from Candida antarctica
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