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Immobilization of enzymatic extract from Penicillium camemberti with lipoxygenase activity onto a hybrid layered double hydroxide

Paper ID Volume ID Publish Year Pages File Format Full-Text
4059 206 2009 6 PDF Available
Title
Immobilization of enzymatic extract from Penicillium camemberti with lipoxygenase activity onto a hybrid layered double hydroxide
Abstract

A Zn/Al layered double hydroxide was synthesized by alkaline co-precipitation with azelate ions (−OOC(CH2)7COO−). The interlayer space of the layered material is occupied by organic ions as confirmed by X-ray diffraction and FTIR spectroscopy. The resulting hybrid material was tested as support for Penicillium camemberti enzymatic extract, containing lipoxygenase (LOX) activity. The optimal condition for LOX immobilization is done with 0.6 mol L−1 potassium phosphate buffer and pH 6.0. The affinity for the substrate is the same after immobilization, however the specific activity slightly decreases. The immobilization enhanced the thermal stability, which was evident with incubation at 60 °C where the immobilized enzyme retains 68% of specific activity while the free enzyme is inhibited. Recycling assays showed that after eight reaction cycles, the immobilized enzyme retains 60% of the activity.

Keywords
Enzyme; Microbial; Immobilized; Lipoxygenase; Composite
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Immobilization of enzymatic extract from Penicillium camemberti with lipoxygenase activity onto a hybrid layered double hydroxide
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 48, Issue 1, 15 December 2009, Pages 93–98
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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