Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate

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...

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Published inBioprocess and biosystems engineering Vol. 43; no. 12; pp. 2253 - 2268
Main Authors de Souza, Ticiane C., de Sousa Fonseca, Thiago, de Sousa Silva, Jouciane, Lima, Paula J. M., Neto, Carlos A. C. G., Monteiro, Rodolpho R. C., Rocha, Maria Valderez P., de Mattos, Marcos C., dos Santos, José C. S., Gonçalves, Luciana R. B.
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer Berlin Heidelberg 01.12.2020
Springer Nature B.V
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Summary: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. Graphic abstract
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ISSN:1615-7591
1615-7605
DOI:10.1007/s00449-020-02411-8