Sucrose hydrolysis by gelatin-immobilized inulinase from Kluyveromyces marxianus var. bulgaricus
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Elsevier B.V.
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Resumo
The crude cell-free medium from a culture of Kluyveromyces marxianus var. bulgaricus was immobilized in a gelatin-water support, with an immobilization yield of 82.60% for inulinase activity. The optimum pH for both free and immobilized inulinase was the same (3.5) and the optimum temperatures were 55 degrees C for the free and 60 degrees C for the immobilized enzyme. The Arrhenius plots were linear and activation energies were 56.20 (free enzyme) and 20.27 kj/mol K (immobilized enzyme). The kinetic parameters were calculated by Lineweaver-Burk plots and the V-max and K-m were 37.60 IU/mg protein and 61.83 mM for the free inulinase and 31.45 IU/mg protein and 149.28 mM for the immobilized enzyme, respectively. The operational stability of the immobilized inulinase was studied in a continuous fixed-bed column reactor for 33 days, at the end of which the sucrose conversion was 58.12%. (c) 2008 Elsevier Ltd. All rights reserved.
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immobilization, inulinase, inverted sugar, Kluyveromyces marxianus var. bulgaricus
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Inglês
Citação
Food Chemistry. Oxford: Elsevier B.V., v. 111, n. 3, p. 691-695, 2008.
