WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7150
Browse
2 results
Search Results
Now showing 1 - 2 of 2
Article Citation - WoS: 23Citation - Scopus: 26Partial Purification and Preparation of Bovine Lactoperoxidase and Characterization of Kinetic Properties of Its Immobilized Form Incorporated Into Cross-Linked Alginate Films(Elsevier Ltd., 2007) Mecitoğlu, Çiğdem; Yemenicioğlu, AhmetLactoperoxidase (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.Article Citation - WoS: 125Citation - Scopus: 147Incorporation of Partially Purified Hen Egg White Lysozyme Into Zein Films for Antimicrobial Food Packaging(Elsevier Ltd., 2006) Mecitoğlu, Çiğdem; Yemenicioğlu, Ahmet; Arslanoğlu, Alper; Elmacı, Zehra Seda; Korel, Figen; Çetin, Ali EmrahLysozyme, partially purified from hen egg white by precipitation of non-enzyme protein with ethanol and lyophilized after dialysis, was incorporated into zein films. The recovery and specific activity of the enzyme after partial purification varied between 45% and 72% and 2173 and 3448 U/mg, whereas the activity of the lyophilized enzyme varied between 2900 and 3351 U/mg. The partially purified enzyme was very stable and lost almost no activity in lyophilized form or in zein films stored at -18 and 4°C for up to 8 and 4 months, respectively. During partial purification and in zein film preparation, ethanol treatment caused 123-137% and 132-315% activation of the enzyme, respectively. In zein films incorporated with 187-1318 U/cm2 (63-455 μg/cm2) lysozyme, the release rates at 4°C, changed between 7 and 29 U/cm2/min, increased at high lysozyme concentrations. Zein films incorporated with partially purified lysozyme showed antimicrobial effect on Bacillus subtilis and Lactobacillus plantarum. By the addition of disodium EDTA, the films also became effective on Escherichia coli. The results of this study showed that the partially purified lysozyme may be used in antimicrobial packaging to increase food safety.