Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection

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Department: search.filters.department.İzmir Institute of Technology. Food EngineeringSubject: search.filters.subject.Thermal stability

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  • Article
    Citation - WoS: 98
    Citation - Scopus: 118
    Antioxidant Activity of Protein Extracts From Heat-Treated or Thermally Processed Chickpeas and White Beans
    (Elsevier Ltd., 2007) Arcan, İskender; Yemenicioğlu, Ahmet; Yemenicioğlu, Ahmet; 03.08. Department of Food Engineering; 03. Faculty of Engineering; 01. Izmir Institute of Technology
    In this study, antioxidant activities of water-soluble protein extracts from chickpeas and white beans were investigated. The area under the curve (AUC) values of lyophilized crude protein extracts (dialyzed or undialyzed) from thermally processed (121 °C for 20 min) or heat-treated (90 °C for 20 min) chickpeas (73-91 μmol trolox/g) and white beans (39-67 μmol trolox/g) indicated a higher free radical-scavenging capacity and thermostability for chickpea proteins than for white bean proteins. The thermal processing also increased the Fe+2-chelating capacity of lyophilized chickpea crude protein extracts 1.8-fold whereas it caused a 2.3-fold reduction in the Fe+2-chelating capacity of lyophilized white bean crude protein extracts. Dialysis increased the protein content of lyophilized chickpea extracts 1.5-2-fold but it did not affect the protein content of lyophilized white bean extracts significantly. Ammonium sulfate precipitation was not effective for selective precipitation of antioxidant proteins. However, it improved the free radical-scavenging capacity of lyophilized protein extracts from thermally processed chickpeas and white beans by almost 25% and 100%, respectively. DEAE-cellulose chromatography, indicated the presence of five (A1-A5) and three (B1-B3) antioxidant protein fractions in heat-treated and thermally processed chickpea protein extracts, respectively, and can be used for the partial purification of antioxidant proteins. The results of this study showed the good potential of chickpea proteins as thermostable natural food antioxidants.
  • Article
    Citation - WoS: 11
    Citation - Scopus: 16
    Partial Purification of Hen Egg White Lysozyme by Ethanol Precipitation Method and Determination of the Thermal Stability of Its Lyophilized Form
    (Türkiye Klinikleri Journal of Medical Sciences, 2007) Gemili, Seyhun; Umdu, Emin Selahattin; Alsoy Altınkaya, Sacide; Üstok, Fatma Işık; Yener, Fatih Yalçın Güneş; Yemenicioğlu, Ahmet; Altınkaya, Sacide; Yemenicioğlu, Ahmet; 03.02. Department of Chemical Engineering; 03.08. Department of Food Engineering; 03. Faculty of Engineering; 01. Izmir Institute of Technology
    Lysozyme was partially purified from hen egg white by precipitation of non-lysozyme protein impurities during incubation in the prence of ethanol. The thermal stability of the obtained partially purified enzyme was also characterized. The incubation of diluted egg white for 2-8 h in the presence of 20% ethanol was not very effective for the partial purification of lysozyme by precipitation of major egg white proteins; however, 4- to 6-h or 6-h to 8-h incubation of diluted egg white in the presence of 30% and 40% ethanol could be employed more effectively for partial purification of lysozyme. Without applying the incubation period, the highest specific activity was obtained by the treatment of egg white with 40% ethanol. Thus, ethanol at this concentration could be used for a continuous process of partial purification. For batch lysozyme purification, on the other hand, incubation in the presence of 30% ethanol was more appropriate. The activities and protein contents of dialyzed and lyophilized enzymes obtained by 6 h-incubation in the presence of 20%, 30%. and 40% ethanol precipitations were 1878, 6669, and 6115 U/mg powder, and 0.98, 0.90, and 0.93 mg protein per mg powder, respectively. The ranges of thermal inactivation parameters, such as D (D80°C = 29.2-59 min, D90°c = 8.8-21 min) and z (Z80-90°c = 17.4-22.3 °C) values of the enzyme, clearly indicated the moderate and variable heat stability of lyophilized lysozymes obtained from different batches of egg white.