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Abstract

Mucor miehei lipase was immobilized on magnetic polysiloxane—polyvinyl alcohol particles by covalent binding with high activity recovered. The performance of the resulting immobilized biocatalyst was evaluated in the synthesis of flavor esters using heptane as solvent. The impact on reaction rate was determined for enzyme concentration, molar ratio of the reactants, carbon chain length of the reactants, and alcohol structure. Ester synthesis was maximized for substrates containing excess acyl donor and lipase loading of 25 mg/mL. The biocatalyst selectivity for the carbon chain length was found to be different concerning the organic acids and alcohols. High reaction rates were achieved for organic acids with 8 or 10 carbons, whereas increasing the alcohol carbon chain length from 4 to 8 carbons gave much lower esterification yields. Optimal reaction rate was determined for the synthesis of butyl caprylate (12 carbons). Esterification performance was also dependent on the alcohol structure, with maximum activity occurring for primary alcohol. Secondary and tertiary alcohols decreased the reaction rates by more than 40%.

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Correspondence to Heizir F. de Castro .

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Bruno, L.M., de Lima Filho, J.L., de M. Melo, E.H., de Castro, H.F. (2004). Ester Synthesis Catalyzed by Mucor miehei Lipase Immobilized on Magnetic Polysiloxane-Polyvinyl Alcohol Particles. In: Finkelstein, M., McMillan, J.D., Davison, B.H., Evans, B. (eds) Proceedings of the Twenty-Fifth Symposium on Biotechnology for Fuels and Chemicals Held May 4–7, 2003, in Breckenridge, CO. Biotechnology for Fuels and Chemicals. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-837-3_17

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  • DOI: https://doi.org/10.1007/978-1-59259-837-3_17

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-4684-9873-8

  • Online ISBN: 978-1-59259-837-3

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