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Immobilization of an enzymatic extract from Penicillium camemberti containing lipoxygenase and hydroperoxide lyase activities

Abstract : An enzymatic extract from Penicillium camemberti, containing lipoxygenase (LOX) and hydroperoxide lyase (HPL) activities, was immobilized on oxirane acrylic beads, Eupergit C and Eupergit C250L-iminodiacetic acid (IDA). The optimum pH for LOX activity was determined to be 4.0 and 6.0 for the free enzyme extract and 6.0 for the immobilized one, whereas that for the HPL activity was 4.0 and 6.0 for the immobilized and free extracts. The optimal reaction temperature for LOX activity was 30 and 55 °C for the free and immobilized enzyme extracts, respectively, whereas the HPL activity showed its optima at 45 and 30 °C, for the free and immobilized extracts, respectively. The immobilization of the enzymatic extract dramatically enhanced the thermostability of LOX and HPL activities. In term of enzymatic stability, the lyophilized immobilized extract showed that its HPL activity at 4 °C was more stable than that of LOX. The results indicated a decrease and an increase in enzyme efficiency for LOX and HPL activity, respectively, upon immobilization.
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Submitted on : Wednesday, February 5, 2020 - 11:33:23 AM
Last modification on : Thursday, June 18, 2020 - 12:32:06 PM

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Colin Eric Hall, Salwa Karboune, Florence Husson, Selim Kermasha. Immobilization of an enzymatic extract from Penicillium camemberti containing lipoxygenase and hydroperoxide lyase activities. Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2008, 52-53, pp.88-95. ⟨10.1016/j.molcatb.2007.11.002⟩. ⟨hal-02467785⟩

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