Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzyma
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RESEARCH PAPER
Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco‑friendly support for enzymatic kinetic resolution of rac‑indanyl acetate Ticiane C. de Souza1 · Thiago de Sousa Fonseca2 · Jouciane de Sousa Silva1 · Paula J. M. Lima1 · Carlos A. C. G. Neto1 · Rodolpho R. C. Monteiro1 · Maria Valderez P. Rocha1 · Marcos C. de Mattos1 · José C. S. dos Santos1,3 · Luciana R. B. Gonçalves1 Received: 14 May 2020 / Accepted: 15 July 2020 © Springer-Verlag GmbH Germany, part of Springer Nature 2020
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.
* José C. S. dos Santos [email protected]
Rodolpho R. C. Monteiro [email protected]
* Luciana R. B. Gonçalves [email protected]
Maria Valderez P. Rocha [email protected]
Ticiane C. de Souza [email protected]
Marcos C. de Mattos [email protected]
Thiago de Sousa Fonseca [email protected]
1
Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE CEP 60455760, Brazil
2
Departamento de Química Orgânica e Inorgânica, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE CEP 60455970, Brazil
3
Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, Redenção, CE CEP 62785000, Brazil
Jouciane de Sousa Silva [email protected] Paula J. M. Lima [email protected] Carlos A. C. G. Neto [email protected] http://lattes.cnpq.br/1706953474706456
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Vol.:(0123456789)
Bioprocess and Biosystems Engineering
Graphic abstract
Keywords CALB · Eco-friendly support · Modulation of lipase · Enzymatic kinetic resolution
Introduction The drawbacks related to the industrial use of soluble enzymes may be overcome by the immobilization on solid supports, for example, producing heterogeneous biocatalysts [1–5]. The different mechanisms of enzyme-support modulation aim at the formation of more stable biocatalysts in face of possible app
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