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Accurel MP 1000 as a support for the immobilization of lipase from Burkholderia cepacia: Application to the kinetic resolution of myo-inositol derivatives

Authors:José Cleiton Sousa dos Santos, Roberto Fernandez-Lafuente
Groups of research:Optimization of biocatalysts and bioprocesses
Evelin A. Manoela,b, Marcela F. P. Ribeiroa, c, Jose C. S. dos Santosd,e, Maria Alice Z. Coelhob, Alessandro B. C. Simasf, Roberto Fernandez-Lafuente*,e  and Denise M. G. Freire*,f
a Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, Faculdade de Farmácia, Departamento de Biotecnologia Farmacêutica, Centro de Ciências e Saúde, Bloco B, 1 andar (1 floor), Laboratório Multidisciplinar de Pesquisas em Biotecnologia, cep: 21941902.
b Universidade Federal do Rio de Janeiro, Ilha do Fundão, Rio de Janeiro, RJ, Brazil, EQ, Departamento de Engenharia Bioquímica;
c Programa de Pós-Graduação em Bioquímica/Instituto de Química, Universidade Federal do Rio de Janeiro, Ciudade Universitária, Centro de Tecnologia, Bloco A, 70 Andar, Rio de Janeiro, 21941-909 RJ, Brazil
dDepartamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455-760, Fortaleza, CE, Brazil
e Department  of biocatalysis. ICP-CSIC. Campus UAM-CSIC. Cantoblanco. 28049 Madrid. Spain
fNúcleo de Pesquisas de Produtos Naturais, Universidade Federal do Rio de Janeiro, Cidade Universitária, Centro de Ciências da Saúde, Bloco H, Rio de Janeiro, 21941-902 RJ, Brazil
Lipase from Burkholderia cepacia (PS) has been immobilized on Accurel MP 1000, and their performance has been compared to that of the most widely used immobilized commercial preparation of this enzyme. The maximum loading was 18 mg protein/g support, and its thermal and solvent stability was much higher than that of the commercial. PS preparations were used in hydrolysis of triacetin and methyl mandelate, in the esterification of oleic acid and ethanol and in the kinetic resolution of 1,3,4-tri-O-benzyl-myo-inositol (DL-1) using vinylacetate as activated acyl donor.  For all reactions studied, PS on Accurel was more active than PS-IM. The conversion in the kinetic resolution of racemic DL-1 was optimized using response surface methodology. Optimal conditions were determined to be 2.0 mg/mL of substrate, temperature of 40oC, 2.0 ml of vinyl acetate and without water addition. Under these conditions, maximum loaded Accurel-PS preparation permitted to improve the activity in this kinetic resolution compared to the PS commercial preparation by a 55 fold factor, and compared to Novozym 435 (the most active described in literature for this reaction) by a 23 fold factor. The conversion attained was 49.9% ± 0.3 of conversion and ee of 99% after 24 hours. The reusability studies showed maintenance of conversion and ee during eight cycles. 

Keywords:3, Hydrophobic supports, interfacial activation, tuning lipase properties, lipase immobilization-stabilization, solvent free reaction medium, resolution of 1, 4-tri-O-benzyl-myo-inositol.
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