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Bioprocess Biosyst Eng ; 43(12): 2253-2268, 2020 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-32725440

RESUMO

In this study, the modulation of enzymatic biocatalysts were developed by the use of lipase B from Candida antarctica covalently immobilized on an eco-friendly support, cashew apple bagasse, activated with 10% glycidol-ethylenediamine-glutaraldehyde (GEG) under different immobilization strategies (5 mM or 100 mM ionic strength and in absence or presence of 0.5% (v/v) Triton X-100). The biocatalysts were characterized for thermal and organic solvents stabilities and compared with the soluble enzyme. The biocatalysts were then applied to the hydrolysis of the rac-indanyl acetate (2:1 ratio enzyme/substrate) at pH 7.0 and 30 °C for 24 h. For all the strategies evaluated, GEG promoted kinetic resolution of rac-indanyl acetate with maximum conversion (50%) and led to (R)-indanol with excellent enantiomeric excess (97%), maintaining the maximum conversion for five consecutive cycles of hydrolysis. Therefore, the use of cashew apple bagasse has proved to be a promising eco-friendly support for enzyme immobilization, since it resulted in stable biocatalysts for enzymatic kinetic resolution.


Assuntos
Acetatos/química , Basidiomycota/enzimologia , Proteínas Fúngicas/química , Lipase/química , Anacardium/metabolismo , Candida/enzimologia , Estabilidade Enzimática , Enzimas Imobilizadas/química , Etilenodiaminas/química , Glutaral/química , Concentração de Íons de Hidrogênio , Cinética , Bases de Schiff , Solventes/química , Estereoisomerismo , Temperatura , Fatores de Tempo
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