TR Dizin İndeksli Yayınlar / TR Dizin Indexed Publications Collection
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Article Citation - WoS: 8Citation - Scopus: 7Commercially Suitable Pectin Methylesterase From Valencia Orange Peels(Türkiye Klinikleri Journal of Medical Sciences, 2010) Şimşek, Şebnem; Yemenicioğlu, AhmetA simple and effective procedure was developed to extract pectin methylesterase (PME) from Valencia orange peels. Orange peels contain 25-34 μmol of COOH min-1 g-1 of peel PME activity. The enzyme was ionically bound to cell walls and could not be extracted with water. This enables removal of water soluble pectic substances and oils from peels via homogenization and washing with water before enzyme extraction. Enzyme extraction can be conducted simply by addition of suitable amounts of NaCl (optimum: 10 g of NaCl 100 g-1 of extraction mixture) to peel homogenate and stirring (optimum: 30 min at 200 rpm). The PME extracted from orange peels contains almost the same amount of heat-stable and heat-labile fraction, and the enzymes cannot be activated by mild heating. A slight activation of enzyme (almost 20%) was achieved by adding 1 mM CaCl2 to enzyme extracts, but this agent was inhibitory at higher concentrations. The extracts stabilized by Na-benzoate and K-sorbate maintained more than 90% of their PME activity at 4 °C for at least 5 months. The obtained PME was successfully used to prepare low-methoxyl citrus pectin used in edible film formation in the presence of CaCl2. This study shows the potential of using Valencia orange peels as a source of commercial PME. © TÜBİTAK.Article Citation - WoS: 11Citation - Scopus: 16Partial 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; Yaprak, Nilgün; Üstok, Fatma Işık; Yener, Fatih Yalçın Güneş; Mecitoğlu Güçbilmez, Çiğdem; Altınkaya, Sacide; Yemenicioğlu, AhmetLysozyme 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.