Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/2261
Title: Partial purification and preparation of bovine lactoperoxidase and characterization of kinetic properties of its immobilized form incorporated into cross-linked alginate films
Authors: Mecitoğlu, Çiğdem
Yemenicioğlu, Ahmet
Mecitoğlu, Çiğdem
Yemenicioğlu, Ahmet
Izmir Institute of Technology. Food Engineering
Keywords: Alginate films
Antimicrobial packaging
Characterization
Immobilization
Lactoperoxidase
Issue Date: 2007
Publisher: Elsevier Ltd.
Source: Mecitoğlu, Ç., and Yemenicioğlu, A. (2007). Partial purification and preparation of bovine lactoperoxidase and characterization of kinetic properties of its immobilized form incorporated into cross-linked alginate films. Food Chemistry, 104(2), 726-733. doi:10.1016/j.foodchem.2006.11.074
Abstract: Lactoperoxidase (LPS), purified directly from bovine rennet whey by Toyopearl-SP cation-exchange chromatography and lyophilized by using dextran as supporting material, maintained almost 70 and 60% of its activity after almost 2 and 5 months storage at -18 °C, respectively. Incorporation of the prepared LPS into alginate films between 0.08 and 0.69 mg/cm2 (516-4325 U/cm2) caused the immobilization of most of the enzyme and gave films with LPS activity between 0.05 and 2.8 U/cm2, determined in the presence of 8 μM H2O2. Between 2 and 24 μM H2O2 concentrations, a two-fold increase in H2O2 concentration caused 1.5-2.5-fold increase in LPS activity of films incorporated with 0.24-0.28 mg/cm2 (1200 U/cm2) LPS. The Q10 and Ea of immobilized enzyme activity between 4 and 16 °C were 1.69 and 34.6 kJ/mol, respectively. However, in the 16-30 °C range, the temperature change had almost no effect on LPS activity of films. The optimal activity of immobilized LPS was observed at pH 6.0, but the enzyme maintained 30-85% of its activity between pH 3.0 and 7.0. The immobilized LPS also had a high stability between pH 4.0 and 6.0. The results of this study showed the good potential of LPS-incorporated alginate films in forming a natural antimicrobial mechanism in different foods.
URI: http://doi.org/10.1016/j.foodchem.2006.11.074
http://hdl.handle.net/11147/2261
ISSN: 0308-8146
0308-8146
Appears in Collections:Food Engineering / Gıda Mühendisliği
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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