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- W2766964110 abstract "Nowadays, for the industrial implementations, especially in the area of organic synthesis, immobilized enzymes are preferred over their soluble forms. Present study aimed to find fast, cost-efficient, and effective way of lipase immobilization for the use in organic media. Lipase from Aspergillus sp. (Resinase A 2X) was immobilized utilizing cross-linking of enzyme aggregates, covalent immobilization on magnetite particles and adsorption-immobilization using pyrolyzed sugar industry waste product as a novel type of carrier. Covalently- and adsorption-immobilized preparations exhibited greater specific activities (5.61 ± 0.18 U/mg and 14.2 ± 0.63 U/mg, respectively) in organic reaction media than the soluble form of the enzyme (0.06 ± 0.01 U/mg). Enzyme immobilized on the sugar industry waste pyrolyis product was determined as a best way to hyperactivate Resinase A 2X and was chosen for the synthesis of flavor and fragrance compound 2-phenylethyl butanoate. Furthermore, in order to optimize 2-phenylethyl butanoate synthesis conditions, central compositional experimental plan was designed using RSM. It showed that in optimal reaction conditions (4.5 h at 40.7 °C, with 0.1 M of substrate) conversion higher than 90% can be achieved. Studies of the operational stability showed enhanced reusability of adsorption-immobilized lipase (with each cycle, efficiency of the 2-PB synthesis diminished by 20–30%). The use of the sugar industry waste pyrolysis product as a carrier provides a novel, cheap, fast, cost-efficient and eco-friendly way of immobilization with some crucial points to be noted for the best productivity." @default.
- W2766964110 created "2017-11-10" @default.
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- W2766964110 date "2018-03-01" @default.
- W2766964110 modified "2023-09-26" @default.
- W2766964110 title "Analysis of Aspergillus sp. lipase immobilization for the application in organic synthesis" @default.
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- W2766964110 doi "https://doi.org/10.1016/j.ijbiomac.2017.11.010" @default.
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