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Purification, Immobilization, and Characterization of Bovine Lactoperoxidase Publisher



Jafary F1 ; Kashanian S2 ; Samsam Sharieat SZ3
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Authors Affiliations
  1. 1. Department of Biology, Faculty of Science, Razi University, Kermanshah, Iran
  2. 2. Faculty of Chemistry, Nanoscience and Nanotechnology Research Center (NNRC), Razi University, Kermanshah, P.O. Box 67149, Iran
  3. 3. Department of Clinical Biochemistry, Isfahan University of Medical Sciences, Isfahan, Iran

Source: International Journal of Food Properties Published:2013


Abstract

Enzyme immobilization is an effective method to improve enzyme properties. There are varieties of immobilization techniques. In this study, lactoperoxidase was purified using different chromatography techniques. Polyaniline polymer was used due to its unique physical and chemical properties to immobilize lactoperoxidase. Polyaniline polymer was activated with glutaraldehyde first, and then lactoperoxidase was successfully immobilized on it. Then the effects of enzyme concentration, time, and pH on the immobilization efficiency were investigated. The bare polyaniline polymer and polyaniline polymer-enzyme surface topographies were investigated via atomic force microscope. Calculated binding efficiency showed that immobilized lactoperoxidase conserved 91% of its native activity. Also, stability studies showed that the stability of immobilized enzyme in comparison with free enzyme was increased; moreover, the immobilized enzyme can be reused for several times without loss of activity. Copyright © Taylor & Francis Group, LLC.
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