Sürdürülebilir Kalkınma Amaçları
Yazarlar
- Demir, Nazan(5)
- Demir, Yasar(3)
- Nadaroglu, Hayrunnisa(3)
- Tasgin, Esen(3)
- Adiguzel, Ahmet(2)
- Gulluce, Medine(2)
- Güllüce, Medine(2)
- Çelik, Safinur Yildirim(2)
- Adigüzel, Ahmet(1)
- Celik, Safinur Yildirim(1)
- Chafik, Abdelbasset(1)
- Essamadi, Abdelkhalid(1)
- Isik, Ceyhun(1)
- Mavi, Ahmet(1)
- Nadaroǧlu, Hayrunnisa(1)
- Ozkan, Asuman(1)
- Taşkin, Esen(1)
Yayınlar
- MakaleYalnız künye2019Scopus SJRQ1Purification and biochemical characterization of a novel copper, zinc superoxide dismutase from liver of camel (Camelus dromedarius): An antioxidant enzyme with unique properties
Chafik, Abdelbasset; Essamadi, Abdelkhalid; Çelik, Safinur Yildirim; Mavi, Ahmet
A novel copper, zinc superoxide dismutase (CuZnSOD) was purified to homogeneity from the liver of an animal well adapted to the stressful living conditions of the desert, the camel (Camelus dromedarius). The biochemical properties of camel liver CuZnSOD were examined. The purified enzyme had a native molecular weight of 28 kDa, as judged by gel filtration chromatography, and showed a single band at 27 kDa on SDS-PAGE, indicating that it is a monomeric protein. Optimal activity of the purified enzyme occurred at 43 °C and pH 6.0, and the activation energy was 1.42 kJ/mol. CuZnSOD activity was strongly inhibited by β-ME, DTT, H 2 O 2 and SDS and slightly inhibited by EDTA, NaN 3 and PMSF. Al 3+ , Ca 2+ , Cd 2+ , Mg 2+ and Zn 2+ stimulated CuZnSOD activity, whereas Ba 2+ , Co 2+ , Fe 2+ and Ni 2+ inhibited it. The purified enzyme contained 0.010 µg of Cu and 0.69 µg of Zn per mg of protein. K m , V max , k cat and k cat /K m values for NBT and riboflavin were 16.27 and 0.16 µM, 20.85 and 21.54 U/mg, 9.65 and 9.97 s −1 , and 0.59 and 62.33 s -1 µM −1 , respectively. Camel liver CuZnSOD exhibited unique biochemical properties compared to those of other CuZnSODs, including lower molecular weight with a monomeric structure, higher optimum temperature, very low E a , very low optimum pH, very low contents of Cu and Zn, and higher affinity, turnover number and catalytic efficiency for riboflavin. These unique properties of camel liver CuZnSOD might be related to the ability of this animal to inhabit stressful desert conditions.
AtıfScopus26WoS23OpenAlex26
İncele - MakaleAçık Erişim2014Production of pectin lyase from Geobacillus pallidus p26, purification, characterization and fruit juice application
Çelik, Safinur Yildirim; Demir, Nazan; Demir, Yasar; Adiguzel, Ahmet; Gulluce, Medine
A bacterial strain was isolated from Pasinler hot spring, Erzurum, Turkey. The purified thermophilic isolate was identified as Geobacillus pallidus P26 and used to produce extracellular pectin lyase (EC 4.2.2.10). Pectin lyase enzyme was purified 34 fold by using DEAE-cellulose anion exchange column chromatography and characterized. Molecular weight of the enzyme was determined as 56 kDa by using Sephadex G-100 gel filtration chromatography. Purification of enzyme was verified by SDS-PAGE. The pH- and temperature optima of enzyme were determined (pH 9.0 and 60 degrees C, respectively). Pectin lyase was mostly stable at 50 degrees C: for 24 hours. Its' activity ducruitscd to 50 % for 24 h at 60 degrees C. K-M and V-max were calculated as 24.8 mg/mL and 2.28 mu mol/L min, respectively. Purified pectin lyase was inhibited by Fe3+, Zn2+, Cu2+, Ca2+, Co2+ and Hg2+ but not by Mg2+. The purified pectin lyase enzyme was used for getting fruits juices. It was found that yields of fruits juices increased when they were compared with control.
AtıfWoS9OpenAlex9İncele - MakaleYalnız künye2014Scopus SJRQ2Purification of paraoxonase enzyme from the sera of patients with behcet’s disease and analyzing the effects of the drugs containing imuran (azathioprine), prednisolone (methylprednisolone) and colchium (colchicine)
Demir, Nazan; Nadaroglu, Hayrunnisa; Ozkan, Asuman; Tasgin, Esen; Isik, Ceyhun; Demir, Yasar
In this study, serum samples from 50 patients with the diagnosis of Behcet’s disease and 20 healthy volunteers were analyzed. The study consists of three parts. In the first part, paraoxonase (PON) activities were determined in the serum samples of 50 patients with Behcet’s disease and 20 healthy people. In the second part, equal volumes of serum samples from 50 patients were pooled and PON enzymes were purified by using Sepharose-4B-L-tyrosine tyrosine-1-naphtylamine affinity column. Optimum temperature, optimum pH, Vmax and Km values of the pure enzymes were determined. The same purification procedure was also performed in the serum samples of 20 healthy people. Electrophoretic mobility was observed (via SDS-PAGE) in the PON enzymes that were purified from the serum samples of patients with Behcet’s disease and healthy people. In the third part, in vitro effects of drugs containing azathioprine, methylprednisolone and colchicine that have already been used for the treatment of Behcet’s disease were tested on the PON enzymes of the patients with Behcet’s disease and control group. IC50 values and Ki constant values were measured and inhibition types were determined for the drugs containing azathioprine, methylprednisolone and colchicine that have already been used for the treatment of the Behcet’s disease and demonstrate in vitro inhibition effects.
AtıfScopus2OpenAlex3İncele - MakaleYalnız künye2014Scopus SJRQ4Production of pectin lyase from xanthomonas campestris, purification, characterization and fruit juice application
Celik, Safinur Yildirim; Demir, Yasar; Demir, Nazan; Güllüce, Medine
Extracellular pectin lyase (EC 4.2.2.10) was produced by Xanthomonas campestris in solid state fermentation. Solid state fermentation was carried out using 250 mL Erlenmeyer flasks containing 5 g wheat bran, 1% citrus pectin and 10 mL salt mixture that composed of 0.14% (NH4)2SO4 0.02% MgCl2 and 0.02% K2HPO4. Pectin lyase enzyme was purified 43 fold by using DEAE-cellulose anion exchange column chromatography and characterized. Molecular weight of the enzyme was determined as 77.5 kDa by using Sephadex G-100 gel filtration chromatography. Purification of enzyme was controlled by SDS-PAGE. The optimum pH and temperature of enzyme was determined as pH 9.0 and 50°C, respectively. Pectin lyase was mostly stable 40°C for 24 hours. KM and Vmax were calculated respectively as 0.69 mg/mL and 3.84 |μmol/L∗min. Purified pectin lyase was inhibited by Fe+, Zn2+, Ca2+, Co2+ and Hg2+ except for Cu2+ and Mg2+ The purified pectin lyase enzyme was used for getting fruits juices. It was determined that yields of fruits juices improved when it was compared with control.
- MakaleYalnız künye2013Scopus SJRQ3Purification and characterisation of laccase from lactarius volemus and its application in removal of phenolic compounds from fruit juice
Nadaroglu, Hayrunnisa; Tasgin, Esen
Laccases are multicopper oxidases (EC 1.10.3.2.), widely distributed in fungi, higher plants and bacteria. In this research, a laccase from Lactarius volemus (Russulaceae) was purified by 73.08 fold using precipitate of saturation (NH4)2SO4, DEAE-cellulose and Sephacryl S200. It was shown that purified enzyme was homogeneous in term of SDS-PAGE with molecular mass estimated of 30 kDa. The pH was optimal at 4.0, enzyme was stable at pH 3.0-5.0 and optimal temperature was at 50°C. Cu2+ and Fe2+ were activated to the purified laccase enzyme, and it was partially inhibited by 5 mM concentration of some metal salts and EDTA, urea, SDS, L-cysteine, dithioeritritol and β-mercaptoethanol. In addition, it was investigated whether the purified and characterized laccase enzyme would remove the phenolic compound of some fruit juices which are responsible for haze formation and browning during storage. Their application led to reduction of total phenolic compounds for apple, apricot, cherry and grape juice. As a result, the effect of these enzymatic treatments on total phenol content and clarity of the juice were evaluated using a central composite design. This laccase enzyme had potential application in food processing.
AtıfScopus18İncele - MakaleAçık Erişim2011Scopus SJRQ3Purification and characterization of a pectin lyase produced by Geobacillus stearothermophilus Ah22 and its application in fruit juice production
Demir, Nazan; Nadaroglu, Hayrunnisa; Tasgin, Esen; Adiguzel, Ahmet; Gulluce, Medine
Extracellular pectin lyase (PL) (EC 4.2.2.10) was produced by Geobacillus stearothermophilus Ah22 in solid state fermentation. The PL enzyme was purified 40.8-fold by DEAE-cellulose anion exchange column chromatography and characterized. The molecular weight of the enzyme was determined as 36 kDa by Sephadex G-100 gel filtration chromatography. Purification of the enzymewas verified by SDS-PAGE. The optimumpHand temperature of the enzyme were determined as pH 6.0 and 60°C, respectively. The PL was mostly stable at 40°C. Its activity deceased by 50% after 2 h at 60°C and by 60% after 6 h at 50°C. The V max and K m were calculated as 0.47 mg/mL and 355.3 μmol/L•min, respectively. The presence of 10 mM Ca 2+, Cu 2+, Mn 2+, Mg 2+, Zn 2+, Hg 2+, Fe 2+ and EDTA, L-cysteine and ascorbic acid significantly enhanced enzyme activity. The purified PL enzyme was used in the production of fruit juices; yields of fruits juice improved significantly compared with controls.
AtıfScopus35WoS28OpenAlex28İncele - MakaleYalnız künye2010Scopus SJRQ4Production of a novel pectin lyase from Bacillus pumilus (P9), Purification and characterisation and fruit juice application
Nadaroǧlu, Hayrunnisa; Taşkin, Esen; Adigüzel, Ahmet; Güllüce, Medine; Demir, Nazan
Extracellular pectin lyase (EC 4.2.2.10) was produced by Bacillus pumilus (P9) in solid state fermentation. Pectin lyase enzyme was purified 36.36 fold by using DEAE-cellulose anion exchange column chromatography and characterized. Molecular weight of the enzyme was determined as 25 kDa by using Sephadex G-100 gel filtration chromatography. Purification of enzyme was controlled by SDS-PAGE. The optimum pH and temperature of enzyme was determined as pH 6.0 and 60oC, respectively. Pectin lyase was mostly stable at 40°C. Its' activity deceased in 50% for 1h at 60°C and 40% for 4 h at 50°C. Vmax and KM were calculated respectively as 0.298 mg/mL and 132.6 mol/L*min. The presence of 10 mM concentration of Ca2+, Cu2+, Mn2+, Mg2+, Zn2+, Hg2+, Fe2+ and EDTA, L-cystein, ascorbic acid and -mercaptoethanol significantly enhanced the pectin lyase of the purified enzyme. The purified pectin lyase enzyme was used for getting fruits juices. It was determined that yields of fruits juices significantly improved when it was compared with control.
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