WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7150
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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.Article Citation - WoS: 39Citation - Scopus: 49Production of Antimicrobial Films by Incorporation of Partially Purified Lysozyme Into Biodegradable Films of Crude Exopolysaccharides Obtained From Aureobasidium Pullulans Fermentation(University of Zagreb, 2005) Kandemir, Nilay; Yemenicioğlu, Ahmet; Mecitoğlu, Çiğdem; Elmacı, Zehra Seda; Arslanoğlu, Alper; Göksungur, Mehmet Yekta; Baysal, TanerAntimicrobial films were produced by incorporating partially purified lysozyme into films of crude exopolysaccharides (59% pullulan) obtained from Aureobasidium pullulans fermentation. After film making, the films containing lysozyme at 100, 260, 520 and 780 μg/cm2 showed 23 to 70% of their expected enzyme activities. The highest recovery of enzyme activity (65-70%) after the film making was obtained in films prepared by incorporating lysozyme at 260 μg/cm2 (1409 U/cm2). The incorporation of disodium EDTA·2H2O and sucrose did not affect the initial lysozyme activity of the films significantly. With or without the presence of disodium EDTA·2H2O at 52 or 520 μg/cm2, lysozyme activity showed sufficient stability in the films during 21 days of cold storage. However, the presence of sucrose at 10 mg/cm2 in the films caused the destabilization of part of enzyme activity (almost 35%) at the end of storage. The combinational incorporation of lysozyme at 780 μg/cm 2 (4227 U/cm2) and disodium EDTA·2H2O at 520 μg/cm2 gave antimicrobial films effective on Escherichia coli. However, in the studied lysozyme concentration range the films did not show any antimicrobial activity against Lactobacillus plantarum. This study clearly showed that the partially purified lysozyme and crude exopolysaccharides from Aureobasidium pullulans may be used to obtain antimicrobial films to increase the safety of foods.