Food Engineering / Gıda Mühendisliği

Permanent URI for this collectionhttps://hdl.handle.net/11147/12

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Publisher: search.filters.publisher.Elsevier Ltd.Subject: search.filters.subject.Characterization

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  • Article
    Citation - WoS: 23
    Citation - Scopus: 26
    Partial 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, Ahmet
    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.
  • Article
    Citation - WoS: 21
    Citation - Scopus: 29
    Partial Purification and Kinetic Characterization of Mushroom Stem Polyphenoloxidase and Determination of Its Storage Stability in Different Lyophilized Forms
    (Elsevier Ltd., 2007) Şimşek, Şebnem; Yemenicioğlu, Ahmet
    Monophenolase (1011 ± 626 U/g AP) and diphenolase activities (5163 ± 3059 U/g AP) of PPO in acetone powders (APs) of different mushroom stems varied considerably. However, the limited variation of average dipenolase (L-DOPA) to monophenolase (L-tyrosine) activity ratio (5.4 ± 0.7) in crude extracts showed the homogeneity of PPO from different mushroom stems. The change in extraction material or partial purification method (ammonium sulfate or acetone precipitation) did not affect the temperature stability, temperature and pH dependency and Km of monophenolase activity considerably. However, some changes were observed in pH stability and substrate specificity of PPO in different parties of mushroom stems. The most important aspects of mushroom stem PPO are its lower diphenolase to monophenolase activity ratio than mushroom cap PPO, low temperature dependency of activity between 25 and 40 °C (Ea = 30 kJ/mol), broad optimum pH between 6 and 8, but lack of activity pH ≤5, and ability to use phloridzin as substrate. The mushroom stem PPOs partially purified and lyophilized by using sucrose, dextran or alginate showed moderate to high stability at -18 °C for 6-6.5 months. Thus, the mushroom stems obtained as a waste material during mushroom processing may be used as a more homogenous source than whole mushrooms to obtain PPO used for different industrial, clinical or research purposes.