Abstract
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.
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Acknowledgements
We gratefully acknowledge the financial support of Brazilian Agencies for Scientific and Technological Development, Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico (FUNCAP), project number BP3-0139-00005.01.00/18, Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), project number 422942/2016-2 and 311062/2019-9, Coordenação de Aperfeiçoamento de Ensino Superior (CAPES)—Finance Code 001. M. C. de Mattos thanks CNPq for research sponsorships (Process: 306043/2018-1).
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de Souza, T.C., de Sousa Fonseca, T., de Sousa Silva, J. et al. Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate. Bioprocess Biosyst Eng 43, 2253–2268 (2020). https://doi.org/10.1007/s00449-020-02411-8
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DOI: https://doi.org/10.1007/s00449-020-02411-8