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Öğe Avrupalı seyyahların gözünden Babürlü Sultanı Cihangir döneminde içtimâî hayat(Siirt Üniversitesi, 2019) Aslan, Yakup; Aynakul, GülnisaBabür Şah, 1526 yılında Babürlü Devleti'ni kurmuştur. Babür'ün oğlu Hümayun'un döneminde, 1540-1555 yılları arası Babürlüler Hindistan'ı kaybetmiş olsalar da, daha sonra egemenliklerini yeniden tesis etmişlerdir. Hümayun'un oğlu Ekber dönemi, Babürlü devletinin siyasi, askeri, idari, dini, kültürel ve içtimai yönlerden pekişmesi ve Hindistan'da sağlam temellere dayanması anlamına gelmektedir. Çalışmamızın ana konusu olan Babürlü tarihinin Cihangir dönemi, Ekber döneminde gerçekleştirilen reform ve düzenlemelerin devlet ve toplum nezdinde yansımalarının en iyi şekilde görülebildiği bir devri teşkil etmektedir. Bundan başka Cihangir dönemi Avrupalı seyyahların ticari kaygılarla Hindistan'a akın etmeye başlamaları sebebiyle de ayrı bir önem taşımaktadır. Hazırladığımız bu tezde Hindistan'ı ziyaret etmiş olan yabancı seyyahların Cihangir devri içtimaî hayatına dair görüşleri ve notları değerlendirilmiştir. Thomas Roe, Edward Terry, Francisco Palsaert, William Hawkins, William Finch, Thomas Coryat, John Jourdain, Pietro Della Valle, Joannes De Laet, Fernao Guerreiro, Joseph De Castro gibi Avrupalı seyyahların eserlerinin yanı sıra Cihangirname, Babürname, Hümayunname gibi hatıratlar da kullanılmıştır. Çalışma, giriş bölümü haricinde üç ana bölümden oluşmaktadır. Giriş kısmında tezin konusu, amacı, önemi ve yöntem belirtildikten sonra çalışmada kullanılan kaynaklar verilmiş ve Cihangir'in ölümüne kadar olan Babürlü Devleti'nin siyasi olayları aktarılmıştır. Tezin birinci bölümü, Babürlü ülkesinin genel yapısını ihtiva eden coğrafya, iklim, ticaret ve şehirler ile sürdürülmüştür. İkinci bölümde; din, suçlar-cezalandırmalar, sosyal devlet anlayışı, doğum, eğitim, evlilik, ölüm, giyim-kuşam ve yemekler üzerinden Cihangir dönemi toplumu anlaşılmaya çalışılmıştır. Son bölümde ise Cihangir döneminde gerçekleştirilen törenler, şenlikler, bayramlar ve eğlenceler hakkında bilgi verilmiştir. Durbar, darşan, tartı merasimi, nevruz, hayvan güreşleri, av, bayramlar, çeşitli oyunlar ve diğer birtakım eğlenceler üçüncü bölümde ele alınan konulardan bazılarını oluşturmaktadır. Çalışmamızın sonucunda yabancı seyyahların eserlerinin Cihangir dönemi içtimai hayatının aydınlatılmasındaki önemi ortaya konulmuştur. Ayrıca Babürlülerde dinamik ve çok kültürlü bir sosyal hayatın mevcut olduğu anlaşılmıştır. Özellikle Türk, İslam ve Hinduizm kültürlerinin bir araya gelmesi ile bir Babürlü kültürü meydana gelmiştir.Öğe Chapter 16: Immobilization of Aspergillus niger glucoamylase on epoxy activated Supports(Ekin Publishing House, March, 2019) Aslan, Yakup; Ömerosmanoğlu, Derya; Yaşar, Musa Anter; Turan, Hatice Rumeysa; Dursun, Songül; Yağmur, MehtapFirstly, in the present study, ANGA was covalently immobilized onto Eupergit CM with 100.00 % immobilization and 100.00 % activity yield by optimizing the immobilization conditions. This result is the best between the immobilization studies of ANGA in the literature. Secondly, the immobilized ANGA obtained in this study showed higher usage and storage stabilities than the ANGAs immobilized on another supports in previous studies in the related literature. Thirdly, maltodextrin was completely converted to glucose by using immobilized ANGA. Consequently, it can be said that immobilized ANGA obtained in the present study can be used in the production of glucose syrup from maltodextrin.Öğe Covalent immobilization of an alkaline protease from Bacillus licheniformis(DeGruyter, Aralık, 2018) Aslan, Yakup; Ömerosmanoğlu, Derya; Koç, Eda ÖndülObjective: Since the soluble enzymes can not be used in repeated reactions and are not stable in operational conditions and not suitable for continuous processes, this study aimed the covalent immobilization of Bacillus licheniformis protease (BLP) onto Eupergit CM. Methods: Optimum conditions for immobilization were determined by changing the conditions individually. The proteins and L-tyrosine were determined by UV/VIS spectrophotometer. Results: The immobilization resulted in 100% immobilization and 107.7% activity yields. The optimum pH (7–8) and the optimum temperature (70°C) have not changed after immobilization. The Km values for free and immobilized enzyme were 26.53 and 37.59 g/L, while the Vmax values were 2.84 and 3.31 g L-Tyrosine/L · min, respectively. The immobilized enzyme has not lost its initial activity during the repeated 20 uses and 20 days of storage. The milk proteins were hydrolyzed in 2 h by using immobilized enzyme. The pH of the milk dropped from 6.89 to 6.53, the color was clearer but there was no change in the smell or the taste. Conclusion: Consequently, it can be said that the immobilized BLP obtained can be used for industrial purposes.Öğe Covalent immobilization of aspergillus niger amyloglucosidase (ANAG) with ethylenediamine-functionalized and glutaraldehyde-activated active carbon (EFGAAC) obtained from sesame seed shell(Elsevier, 2020) Sharif, Yousif Mohammed; Şahin, Ömer; Aslan, YakupThis study was aimed the covalently immobilization of Aspergillus niger amyloglucosidase (ANAG) onto activated carbon (AC) obtained from sesame seed shell. AC was firstly functionalized with ethylenediamine, and after then activated with glutaraldehyde. 99.80% immobilization yield and 99.83% activity yield were obtained as the result of optimization of immobilization conditions (pH and molarity of immobilization buffer, AC amount, and reaction time). The optimum pH (5.5) and the optimum temperature range (55–60 C) for ANAG were not affected by immobilization. After immobilization, Vmax value decreased from 1464.1 lmol D-glucose/L.min to 1342.3 lmol D-glucose/L.min, while Km value decreased from 116.3 g maltodextrin/L to 109.9 g maltodextrin/L. The immobilized enzyme retained 99.30% and 98.30% of its initial activity, respectively after twenty repeated uses and after twenty days of storage in 5 mL sodium phosphate buffer (0.1 M, pH 5.5) at +4 C in a refrigerator. Finally, glucose syrup was produced from maltodextrin solution having 1% (w/v) concentration by using the immobilized ANAG. Maltodextrin was completely converted to glucose after four hours. Consequently, it can be said that the immobilized ANAG obtained in this study can be used in the industrial production of glucose syrup.Öğe Covalent immobilization of Aspergillus oryzae ?-galactosidase and Bacillus licheniformis protease with Amino-Multi Walled Carbon Nanotubes(Tarbiat Modares University, 2024) Taher, Alan Yaseen; Alizadeh, Mohammad; Aslan, YakupThis study was carried out with the aim of covalent immobilization of Aspergillus oryzae beta-galactosidase and Bacillus licheniformis protease on multi-walled amino-carbon nanotubes. In this method, fractional 2k design was used to study the effect of seven continuous factors (activation pH, glutaraldehyde molarity, activation time, buffer solution pH, buffer solution molarity, MWCNT-NH3-glutaraldehyde amount and stabilization time) on the stabilization efficiency and enzyme activity. . Design-expert software was used to analyze data and draw graphs. The results showed that the aforementioned factors predict the level of enzyme activity of Bacillus licheniformis protease and Aspergillus oryzae beta-galactosidase with correlation coefficients of 0.80 and 0.92 at the rate of 77 and 88%, respectively. Also, the correlation coefficient of the covalent fixation efficiency model of Aspergillus oryzae beta-galactosidase and Bacillus licheniformis protease on multi-walled carbon nanotubes was 0.89 and 0.82, respectively, and the studied factors were able to determine the covalent fixation beta efficiency, respectively. Aspergillus oryzae galactosidase and Bacillus licheniformis protease on multi-walled amino-carbon nanotubes predict 83 and 77%, respectively. © 2024 Tarbiat Modares University. All rights reserved.Öğe Determination of Some Quality and Safety Parameters for Black Raisin Juice(April, 2019) Aslan, Yakup; Hussein, Hawsar Syamand; Abdullah, Seerwan Ahmed; Cavidoğlu, İsaThe aim of the present study was to determine the safety and the quality parameters of raisin juice, such as total soluble solids (TSS), pH, titratable acidity (TTA), kinds and quantity of sugars, phenolic acid compounds, polyphenoloxidase (PPO) enzyme activity, water activity and total microbial counts. The total soluble solids and pH values were significantly decreased after two weeks of storage, while the titratable acidity in most samples were slightly changed. Glucose, fructose and sucrose as well as three kinds of phenolic acids such as gallic, chlorogenic and vanilic acids were determined in all samples. Total microbial contents of the freshly prepared raisin juice and of the raisin juice stored for one and two weeks did not significantly changed. The water activity was slightly decreased, while the polyphenoloxidase activity was significantly decreased, after storage for two weeks. Consequently, it can be said that the freshly prepared raisin juice and the raisin juice stored for one week have superior sensorial properties than the raisin juice stored for two weeks.Öğe Improved catalytic activity of aspergillus oryzae β-galactosidase by covalent immobilization on eupergit cm(Descember, 2018) Aslan, Yakup; Taher, Alan Yaseen; Cavidoğlu, İsaIn this study, Aspergillus oryzae β-Galactosidase (AOG) was immobilized onto Eupergit CM. By optimizing the immobilization conditions such as pH and molarity of immobilization buffer, enzyme/support ratio and duration of immobilization, 100.00% immobilization yield and 129.82% activity yield was achieved. The optimum temperature (55 °C) of free enzyme was not changed while optimum pH of free enzyme was shifted from 4.5 to 5.5 after immobilization. Kinetic constants for free and immobilized enzyme were also determined by using the Lineweaver-Burk plot. The Km values of the free and immobilized enzymes were determined to be 307.7 and 234.2 g / L respectively, while the Vmax values were determined to be 0.366 g D-Glucose / L.min and 0.415 g D-Glucose / L.min respectively. The operational and storage stabilities of immobilized enzyme were also studied. The activity of immobilized enzyme decreased to 99.3% after repeated twenty usage while decreased to 98.3% after fifteen days of storage. Further, the immobilized enzyme was used for the hydrolyzing the cow's milk lactose. By using the immobilized enzyme, the milk lactose was completely hydrolyzed in four hours. Consequently, immobilized AOG can be used in the industrial production of lactose-free cow's milk.Öğe Improved Performance of Pseudomonas fluorescens lipase by covalent immobilization onto Amberzyme(Turkish Biochem Soc, 2013) Aslan, Yakup; Handayani, Nurrahmi; Stavila, Erythrina; Loos, KatjaObjective: In this study, the conditions of covalent immobilization of Pseudomonas fluorescens lipase onto an oxirane-activated support (Amberzyme) were optimized to obtain a high activity yield. Furthermore, the operational and storage stabilities of immobilized lipase were tested. Methods: Optimum conditions for immobilization were determined by changing individually the conditions (pH from 5 to 9; buffer concentration from 0.025 to 2.5 M; amount of Amberzyme from 100 to 500 mg and duration of immobilization from 24 to 120 h). Amounts of protein and the activity of enzyme were determined by UV/Vis (PYE UNICAM SP8-200 UV/Vis spectrophotometer). Results: Immobilization conditions (pH and molar concentration of immobilization buffer, enzyme/support ratio and immobilization duration) significantly affected the immobilization efficiency. 100% immobilization yield and 145% activity yield were achieved by optimizing the immobilization conditions. Operational and storage stabilities of immobilized lipase were determined as well. The immobilized enzymes retained its activity for 20 consecutive batch reactions. Furthermore, the immobilized lipase showed a high storage stability as no decrease in its activity was observed for 20 days. Conclusion: Our results obtained in the present study are the best in the covalent immobilization of Pseudomonas fluorescens lipase in the literature. Therefore our future studies will focus on using the immobilized Pseudomonas fluorescens lipase for the production of biodiesel, hydrolysis of oils and various important esterification reactions.Öğe Inülinden Fruktooligosakkarit Üretimi için Aspergillus Niger Inülinazının Karboksillenmis Çok Duvarlı Karbon Nano Tüpler ile Kovalent Immobilizasyonu(2021) Aslan, YakupBu projenin konusu, inülinden fruktooligosakkarit (FOS) üretiminde kullanmak için Aspergillus niger inülinaz (ANI) enzimini karboksillenmis çok duvarlı karbon nano tüpler (c-MWCNT) üzerine kovalent baglama yöntemi ile immobilize etmekti. ANI çapraz baglayıcı reaktif glutardialdehit aracılıgıyla c-MWCNT üzerine kovalent baglama yöntemiyle % 100 baglanma verimi ve % 82.6 aktvite verimi ile immobilize edildi. Serbest ve immobilize ANI karakterize edilerek optimum pH, optimum sıcaklık, pH kararlılıgı, ısıl kararlılıgı ve Michaelis-Menten Sabitleri (Km ve Vmax) tayin edildi. Immobilizasyon enzimin optimum pH aralıgını (5.5-6.5) ve optimum sıcaklık aralıgını (55-65 oC) degistirmezken, enzimin pH ve ısıl kararlılıgını artırdı. Immobilize enzimin düsük ve yüksek pH aralıklarında serbest enzime göre daha yüksek aktiviteye ve kararlılıga sahip oldugu görüldü. Immobilizsyon enzimin maksimum hızını ve substrat olarak inüline ilgisini azaltmıstır. Serbest ve immobilize enzimler için elde edilen maksimum hız (Vmax) sırasıyla 3508.8 g/L.dk ve 2890.2 g/L.dk iken ve Km sabiti sırasıyla 662.3 g/L ve 699.3 g/L olarak tayin edildi. Km arttıkça enzimin substrata olan ilgisi azalmaktadır. Immobilize enzim optimum aktivite kosullarında baslangıçtaki aktivitesini pes pese 30 kullanım boyunca korudu. Immobilize enzim optimum depolama kosullarında (bir sonraki kullanıma kadar buzdolabında +4 oC?de 0.1 M?lık ve pH?sı 6.0 olan sodyum fosfat tampunu çözeltisinde depolandı) 20 gün boyunca baslangıçtaki aktivitesini korudu. Immobilize enzim kullanılarak 600 g/L inülin çözeltisinden % 91.15 dönüsüm oranıyla 546.9 g/L derisiminde FOS surubu elde edildi. Sonuç olarak, bu çalısmada elde edilen immobilize enzimin endüstriyel olarak inülinden FOS üretiminde kullanılabilecegi söylenebilir.Öğe The covalent immobilization of ?-galactosidase from Aspergillus oryzae and alkaline protease from Bacillus licheniformis on amino-functionalized multi-walled carbon nanotubes in milk(Cell Press, 2024) Taher, Alan Yaseen; Alizadeh, Mohammad; Aslan, YakupThis study aimed was to covalently immobilize beta-galactosidase from Aspergillus oryzae and protease from Bacillus licheniformis on amino-functionalized multi-walled carbon nanotubes. In this study, a two-level factorial design was employed to investigate the impact of seven continuous variables (activation pH, glutaraldehyde molarity, activation time (0-8 h), buffer solution pH (8-0), buffer solution molarity, MWCNT-NH (2) -glutaraldehyde quantity, and stabilization time (0-180 h)) on the immobilization efficiency and enzymatic activity of protease and beta-galactosidase. Furthermore, the effect of time on the percentage of enzymatic activity was examined during specific intervals (24, 48, 72, 96, and 120 h) of the immobilization process. The analysis of variance results for protease enzymatic activity revealed a notable influence of the seven variables on immobilization efficiency and enzymatic activity. Additionally, the findings indicate that activation time, buffer pH, MWCNT-NH (2) -glutaraldehyde quantity, and stabilization time significantly affect the activity of the protease enzyme. The interplay between buffer pH and stabilization time is also significant. Indeed, both activation time and the quantity of MWCNT-NH (2) -glutaraldehyde exert a reducing effect on enzyme activity. Notably, the influence of MWCNT-NH (2) -glutaraldehyde quantity is more significant (p < 0.05). In terms of beta-galactosidase enzymatic activity, the study results highlight that among the seven variables considered, only the glutaraldehyde molarity, activation time, and the interplay of activation time and the quantity of MWCNT-NH (2) -glutaraldehyde can exert a statistically significant positive impact on the enzyme's activity (p < 0.05). The combination of activation time and buffer solution molarity, as well as the interactive effect of buffer pH and MWCNT-NH2-glutaraldehyde, can lead to a significant improvement in the stabilization efficiency of the protease of carbon nanotubes. The analysis of variance results demonstrated that the efficiency of covalently immobilizing beta-galactosidase from Aspergillus oryzae on amino-functionalized multi-walled carbon nanotubes is influenced by the molarity of glutaraldehyde, buffer pH, stabilization time, and the interplay of activation time + buffer pH, buffer pH + activation time, activation time + buffer molarity, and glutaraldehyde molarity + MWCNT-NH (2) -glutaraldehyde (p < 0.05). Through the optimization and selection of optimal formulations, the obtained results indicate enzyme activities and stabilization efficiencies of 64.09 % +/- 72.63 % and 65.96 % +/- 71.77 % for protease and beta-galactosidase, respectively. Moreover, increasing the enzyme stabilization time resulted in a reduction of enzyme activity. Furthermore, an increase in pH, temperature, and the duration of milk storage passing through the enzyme-immobilized carbon nanotubes led to a decrease in enzyme stabilization efficiency, and lactose hydrolysis declined progressively over 8-h. Hence, the covalent immobilization of beta-galactosidase from Aspergillus oryzae and protease from Bacillus licheniformis onto amino-functionalized multi-walled carbon nanotubes is anticipated to be achievable for milk applications.
