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Evaluation of different methods for immobilization of Candida antarctica lipase B (CalB lipase) in polyurethane foam and its application in the production of geranyl propionate

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Abstract

With the aim of studying the best method for the interaction of polyurethane (PU) foam and Candida antarctica lipase B, different methods of CalB immobilization were studied: adsorption (PU–ADS), bond (using polyethyleneimine) (PU–PEI), ionic adsorption by PEI with cross-linking with glutaraldehyde (PU–PEI–GA) and entrapment (PU). The characterization of immobilized enzyme derivatives was performed by apparent density and Fourier transform infrared spectroscopy. The free enzyme and enzyme preparations were evaluated at different pH values and temperatures. The highest enzyme activity was obtained using the PU method (5.52 U/g). The methods that stood out to compare the stabilities and kinetic parameters were the PU and PU–ADS. Conversions of 83.5 and 95.9 % for PU and PU–ADS derivatives were obtained, in 24 h reaction, using citronella oil and propionic acid as substrates.

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Acknowledgments

The authors thank the financial support of CNPq-Conselho Nacional de Desenvolvimento Científico e Tecnológico and Laboratory of Electronic Micrsocopy (LCME) of Federal University of Santa Catarina for the SEM analyses.

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Authors and Affiliations

  1. Chemical and Food Engineering Department, Federal University of Santa Catarina (UFSC), PO Box 476, Florianópolis, SC, 88040-900, Brazil

    Gabrieli Nicoletti, Eliane P. Cipolatti, Alexsandra Valério, NatáliaThaisa Gamba Carbonera, Nicole Spillere Soares, Eron Theilacker, Jorge L. Ninow & Débora de Oliveira

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  1. Gabrieli Nicoletti
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  2. Eliane P. Cipolatti
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  3. Alexsandra Valério
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  4. NatáliaThaisa Gamba Carbonera
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  6. Eron Theilacker
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  8. Débora de Oliveira
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Correspondence to Débora de Oliveira.

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Nicoletti, G., Cipolatti, E.P., Valério, A. et al. Evaluation of different methods for immobilization of Candida antarctica lipase B (CalB lipase) in polyurethane foam and its application in the production of geranyl propionate. Bioprocess Biosyst Eng 38, 1739–1748 (2015). https://doi.org/10.1007/s00449-015-1415-6

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  • DOI: https://doi.org/10.1007/s00449-015-1415-6

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