Summary
Mucor miehei lipase has been adsorbed on Celite and covalently bound to nylon. The obtained derivatives have been studied regarding their ability for synthetize several flavouring esters in biphasic aqueous/organic media. The influence of the immobilization procedure on the synthetic activity of the derivatives was considered. Solvent hydrophobicity and water content in the biphasic system influenced both enzyme stability and equilibrium displacements. In this way, solvents with log P>3.5 and less than 1% water were optimal. It was important to consider pH effects on enzyme microenvironment when using acidic substrates. Optimum temperature and reuse of the catalyst were also checked.
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Manjón, A., Iborra, J.L. & Arocas, A. Short-chain flavour ester synthesis by immobilized lipase in organic media. Biotechnol Lett 13, 339–344 (1991). https://doi.org/10.1007/BF01027679
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DOI: https://doi.org/10.1007/BF01027679