Food Engineering / Gıda Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/12
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Article Citation - WoS: 36Citation - Scopus: 38Antimicrobial Activity of Lactoperoxidase System Incorporated Into Cross-Linked Alginate Films(John Wiley and Sons Inc., 2009) Yener, Fatih Yalçın Güneş; Korel, Figen; Yemenicioğlu, AhmetIn this study, the antimicrobial effect of lactoperoxidase (LPS) incorporated alginate films was investigated on Escherichia coli (NRRL B-3008), Listeria innocua (NRRL B-33314), and Pseudomonas fluorescens (NRRL B-253) in presence of different concentrations of H2O2 (0.2, 0.4, and 0.8 mM) and KSCN (1, 2, and 4 mM). The incorporation of 70 nmol ABTS/min/cm2 LPS into alginate films gave 0.66 to 0.85 nmol ABTS/min/cm2 enzyme activity at 0.2 to 0.8 mM H2O 2 concentration range. The antimicrobial activity of LPS system on target bacteria changed according to the concentrations of KSCN and H 2O2. The growth of all tested bacteria was prevented for a 6-h period by applying LPS system in presence of 0.4 or 0.8 mM H 2O2 and 4 mM KSCN. At 0.8 mM H2O2 and 4 mM KSCN, the LPS system also inhibited growth of L. innocua and P. fluorescens for a 24-h incubation period, whereas E. coli growth could not be inhibited for 24 h under these conditions. At 0.2 mM H2O2 and 1 to 4 mM KSCN, a considerable inhibitory effect was obtained only on P. fluorescens. The decreasing order of the resistance of studied bacteria to LPS system is as follows: E. coli, L. innocua, and P. fluorescens. The developed antimicrobial system has a good potential for use in meat, poultry, and seafood since alginate coatings are already used in these products. Further studies are needed to test the LPS incorporated edible films in real food systems.Article Citation - WoS: 125Citation - Scopus: 156Antimicrobial and Antioxidant Activity of Edible Zein Films Incorporated With Lysozyme, Albumin Proteins and Disodium Edta(Elsevier Ltd., 2007) Mecitoğlu Güçbilmez, Çiğdem; Yemenicioğlu, Ahmet; Arslanoğlu, AlperIn this study, partially purified lysozyme was incorporated into zein films in combination with chickpea albumin extract (CPAE), bovine serum albumin (BSA) and disodium EDTA. The zein films showed an inherent free radical scavenging activity. Incorporation of lysozyme did not contribute to soluble free radical scavenging activity of zein films. However, the incorporation of lysozyme in combination with CPAE increased the soluble and immobilized free radical scavenging activity of zein films 17% to 25% and almost 84%, respectively. The incorporation of CPAE also improved the distribution of partially purified lysozyme preparation in zein films and enabled the controlled release of lysozyme by reducing its release rate from zein films between 1.5- and 3.5-fold, depending on the concentration of incorporated CPAE. In contrast, the BSA incorporation made distribution of lysozyme more heterogeneous and it did not contribute to the free radical scavenging activity of films significantly. The combinational incorporation of partially purified lysozyme with disodium EDTA · 2H2O or CPAE and disodium EDTA · 2H2O gave zein films effective on Escherichia coli and Bacillus subtilis. This study clearly showed the benefits of using functional protein extracts to control lysozyme distribution and release rate and to improve antioxidant activity in zein films.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.