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- MakaleYalnız künye2023Scopus SJRQ1Ozone and cold plasma: Emerging oxidation technologies for inactivation of enzymes in fruits, vegetables, and fruit juices
Mayookha, V. P.; Pandiselvam, R.; Kothakota, Anjineyulu; Ishwarya, S. Padma; Khanashyam, Anandu Chandra; Kutlu, Naciye; Rifna, E. J.; Kumar, Manoj; Panesar, Parmjit S.; El-Maksoud, Ahmed A. Abd
Inactivation of deteriorative enzymes preserves the quality of fruits and vegetables and extends the shelf-life of fruit juices. Ozonation and cold plasma treatment are recent additions to the thermal and non-thermal methods for enzyme inactivation. However, these techniques stand out in their effectiveness and versatility for the treatment of a wide range of fruits and vegetables. This article appraises the mode of action and applications of ozone and cold plasma for the inactivation of enzymes in fruits, vegetables, and fruit juices. Further, a comprehensive discussion is presented on the influential parameters of enzyme inactivation effectiveness of ozonation and cold plasma processing. Besides, the latter sections of this article highlight the challenges that impose hurdles in the commercial applications of these unconventional techniques and the way forward in improving their efficacy and industrial applications.
AtıfScopus78WoS71OpenAlex70
İncele - MakaleYalnız künye2017Scopus SJRQ1Purification of camel liver catalase by zinc chelate affinity chromatography and pH gradient elution: An enzyme with interesting properties
Chafik, Abdelbasset; Essamadi, Abdelkhalid; Çelik, Safinur Yildirim; Mavi, Ahmet
Climate change and increasing temperatures are global concerns. Camel (Camelus dromedarius) lives most of its life under high environmental stress in the desert and represent ideal model for studying desert adaptation among mammals. Catalase plays a key role in protecting cells against oxidative stress. For the first time, catalase from camel liver was purified to homogeneity by zinc chelate affinity chromatography using pH gradient elution, a better separation was obtained. A purification fold of 201.81 with 1.17% yield and a high specific activity of 1132539.37 U/mg were obtained. The native enzyme had a molecular weight of 268 kDa and was composed of four subunits of equal size (65 kDa). The enzyme showed optimal activity at a temperature of 45 °C and pH 7.2. Thiol reagents, β-Mercaptoethanol and D,L-Dithiothreitol, inhibited the enzyme activity. The enzyme was inhibited by Al3+, Cd2+ and Mg2+, whereas Ca2+, Co2+ and Ni2+ stimulated the catalase activity. Reduced glutathione has no effect on catalase activity. The Km and Vmax of the enzyme for hydrogen peroxide were 37.31 mM and 6185157 U/mg, respectively. Sodium azide inhibited the enzyme noncompetitively with Ki value of 14.43 μM, the IC50 was found to be 16.71 μM. The properties of camel catalase were different comparing to those of mammalian species. Relatively higher molecular weight, higher optimum temperature, protection of reduced glutathione from hydrogen peroxide oxidation and higher affinity for hydrogen peroxide and sodium azide, these could be explained by the fact that camel is able to live in the intense environmental stress in the desert.
AtıfScopus9WoS9OpenAlex10
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