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Öğe Amylase Production of Bacillus subtilis Isolated from Soil by SmF Method(2019) Ortakaya, Veysi; Fincan, Sema AgüloğluIn our study, the isolation, identification and optimization of Bacillus subtilis from soil samples were performedand the ability to produce ?-amylase of industrial importance was investigated. Bacteria identified as B. subtilis by 16SrRNA analysis, morphological and biochemical tests. Maximum growth was determined at 32 hour, 37°C and pH 7.0.Enzyme optimization was performed after determination of bacterial amylase in starchy medium. Optimum conditionsfor amylase production were determined as 37°C, pH 7.0 and 48 h. When the effect of metals on enzyme activity wasexamined, it was determined that Cu2+ increased enzyme activity, Zn2+, Hg2+ and Fe2+ were partially inhibited theenzyme activity, and Ca2+ was showed close activity to the control. It was observed that carbon sources had inhibitoryeffect on bacterial growth and enzyme production.Öğe Innovative hydrogen release from sodium borohydride hydrolysis using biocatalyst-like Fe2O3 nanoparticles impregnated on Bacillus simplex bacteria(Pergamon-Elsevier Science LTD, 2021) Duman, Sibel; Kaya, Bülent; Caf, Fatma; Enez, Barış; Fincan, Sema AgüloğluFor the first time in this innovative study, microorganisms such as Bacillus simplex bacteria, mostly used in biological activity studies, are used as a bio-supporter agent of iron to release hydrogen from sodium borohydride hydrolysis at 25.0 +/- 0.1 degrees C. The goal is to investigate thoroughly sodium borohydride hydrolysis catalyzed by Fe2O3 nanoparticles impregnated on microorganism such as Bacillus simplex (BS) bacteria (Fe2O3@BS NPs) known with strong antibacterial properties, which makes innovative them a candidate for hydrolysis reaction. This study was focused on the preparation, identification, and catalytic use of biocatalyst-like Fe2O3@BS NPs for hydrogen release from the sodium borohydride hydrolysis at 25.0 +/- 0.1 degrees C. The characterization results made after and before hydrolysis reaction using by SEM/SEM-EDX, FT-IR, XRD, UVevis, XPS, DLS, ELS Zeta potential, ESR, and TEM techniques reveal the formation of highly active, stable, durable, and long-lived biocatalysts-like Fe2O3@BS NPs. (c) 2021 Hydrogen Energy Publications LLC. Published by Elsevier Ltd. All rights reserved.Öğe Long Non-Coding RNA H19 Expression in Leukemia Patients(Veysi AKPOLAT, 2023) Aslan, Kadir Sinan; Fincan, Sema AgüloğluAbstract Objective: BCR-ABL fusion gene occurs with the formation of translocations in the t(9;22) region of the Philadelphia (Ph) chromosome, which is used as a diagnostic biomarker in Chronic Myeloid Leukemia (CML). These abnormal genetic changes, which cover 15% of leukemias, reach dimensions that threaten human life. Recent studies have determined that thousands of genes expressed in differentiation and development processes contain non-protein-coding RNA with a regulatory role. Of these, the first discovered long noncoding RNA (LncRNA) H19 has been associated with its biological role, cell proliferation, apoptosis and metastasis Therefore, studies have been conducted considering that LncRNA H19 can be used as a biological marker in CML patients. Method: For this study, blood from 72 CML patients over 18 years of age and 64 healthy individuals were used. After RNA isolation of each of these bloods and cDNAs were obtained, the expression levels of the LncRNA H19 gene were analyzed by Real Time PCR method. Results: As a result of the expression study, it was found that LncRNA H19 gene expression increased 4.37 times and was upregulated in Bcr-Abl positive patients (p=0.414683). Conclusion: In this study conducted in Diyarbakır region, we think that LncRNA H19, which is up-regulated in terms of CML profiles, can be used as a biological marker for new treatment applications.Öğe A novel raw starch hydrolyzing thermostable ?-amylase produced by newly isolated bacillus mojavensis SO-10: Purification, characterization and usage in starch industries(Instituto de Tecnologia do Parana, 2018) Özdemir, Sadin; Fincan, Sema Agüloğlu; Karakaya, Adem; Enez, BarışThe aim of this study is the production, purification, and characterisation of thermostable raw starch hydrolyzing αamylase produced by Bacillus mojavensis SO-10. The maximum production conditions of α-amylase were found at 36th hour, 35 °C and pH 7.0. We utilized three steps to purify the thermostable α-amylase and as a result, 34-fold and 18% yield were obtained. The molecular weight of purified α-amylase was determined as 73 kD. The Km and Vmax rates were detected as 0.010 mM and 3.38 µmol min−1 , respectively. This purified α-amylase exhibited the highest activity at pH 5.0-6.0 and 70 ºC and showed stability over a wide variety of pH and temperature at 4.0–8.0, and 40– 50 ºC, respectively. The thermostable purified α-amylase exhibited stability in the presence of denaturing agents and heavy metal ions. The purified enzyme hydrolyzed the raw starches of corn and wheat grains in the ratio of 36.7% and 39.2% respectively. The end-yields of soluble starch hydrolysis were analyzed by thin-layer chromatography (TLC). In addition, the usage of purified α-amylase in clarification of apple juice and domestic washing detergent industries were evaluated.Öğe The obtainment of alkaline serine protease from Bacillus sp. isolated from solid through the solid-state fermentation technique by using rind of the citrullus lanatus L. (watermelon) and cucumis melo L. (melon)(Dicle Üniversitesi Ziya Gökalp Eğitim Fakültesi, 2007) Fincan, Sema Agüloğlu; Okumuş, VeysiBu çalışmada, ekonomik önemi olmayan ve birikerek çevre kirliliğine yol açan karpuz ve kavun kabuğu katı substrat olarak kullanılarak Katı-Faz Fermentasyonu (SSF) yöntemi ile Bacillus sp.’den yüksek miktarda alkalin serin proteaz eldesi amaçlandı. Enzim aktivitesi üzerine pH, sıcaklık, metaller, azot ve karbon kaynakları etkisi incelendi. Yapılan inhibisyon çalışmasında PMSF ile inhibe olan enzimin alkalin serin proteaz olduğu tespit edildi. SSF yöntemi ekstrasellular enzimlerin düşük masrafla, hızlı bir şekilde, bol miktarda ve çevreye zarar vermeden üretilebildiği bir yöntem olduğu için kullanıldı.Öğe Peynir altı suyundan izole edilen laktik asit bakterisinden ? -amilaz üretimi ve karakterizasyonu(2018) Rezzukoğlu, İhsan; Fincan, Sema Agüloğlu; Enez, BarışBu çalışmada, peynir altı suyundan, ekonomik ve biyoteknolojik olarak fayda sağlamak amacıyla laktik asitbakterileri izole edildi. İzole edilen bakteriler morfolojik, fizyolojik ve biyokimyasal testler yardımıyla tanımlandı.Bakterilerin ekstraselüler ?-amilaz üretme yeteneği araştırıldı. En iyi ? -amilaz aktivitesi gösteren Lactococcus sp. PS2Aile çalışmalara devam edildi.Lactococcus sp. PS-2A bakterisinin kok (yuvarlak) şekilli, Gram pozitif, katalaz negatif, hareketli olduğubelirlendi. Bakteri üremesinin optimum koşulları pH 7.0, 35°C ve 16. saat olarak tespit edildi. Lactococcus sp. PS2A’nınen yüksek ?-amilaz aktivitesini; LB besi yerinde, pH 7.0, 35°C ve 20. saatte gösterdiği belirlendi. Karbonkaynaklarında %1’lik çözünebilir nişastanın ?-amilaz üretimini iki kat arttırdığı saptandı. Azot kaynaklarından %1’likamonyum klorür ile ?-amilaz üretiminin arttığı tespit edildi.Öğe Production of ?-Amylase from Bacillus megaterium MD-1(Bingöl Üniversitesi Fen Bilimleri Enstitüsü, 2022) Fincan, Sema Agüloğlu; Enez, BarışThe alpha-amylase is used extensively in many different industrial sectors and is renowned for modifying starch by rupturing 1-4 glycosidic bands. Depending on the intrinsic properties of the microorganism, several alpha-amylases with thermostable and halotolerant properties are expressed. In the current study, the bacteria were isolated from Ergani Makam Mountain. Identification and optimization of the isolated bacteria were performed. As a result of the 16S rRNA analysis, physiological, morphological and biochemical analyis were carried out for the identification of the isolated microorganism and consequently the bacterium was defined as Bacillus megaterium MD-1. Following its identification, α-Amylase, was isolated from B. megaterium. Optimal conditions for bacteria and enzyme production were determined as 48 hours, 35°C and pH 7.0. Maximum enzyme activity was optained at 40°C and pH 8.0. The effects of various carbon and nitrogen sources on enzyme production were investigated by adding to the nutrient medium. Compared to the control regarding enzyme production, it was determined that carbon sources, particularly sucrose, fructose and lactose inhibited enzyme production by 75%, all carbon sources inhibited production. It was also observed that urea and sodium nitrate from nitrogen sources had an inhibitory effect on enzyme production whereas other nitrogen sources did not. The highest amylase production among nitrogen sources was obtained with peptone addition. In our study, it was determined that an increase in amylase activity could be achieved by using the optimum values of physical parameters. These findings displayed that enzyme could be utilized in fruit juice industries for clarification of apple juice, textile industry and raw starch hydrolyzing.Öğe Production, purification, and characterization of thermostable ?-amylase from thermophilic Geobacillus stearothermophilus(Wiley-V C H Verlag Gmbh, 2014) Fincan, Sema Agüloğlu; Enez, BarışThe -amylase (-1-4-D-glucan glucanohydrolase; EC 3.2.1.1) secreted by Geobacillus stearotermophilus was purified and characterized. Maximum enzyme production was achieved after 24h cultivation at pH 7.0 and 55 degrees C. The enzyme was active in a broad temperature range, between 50 and 80 degrees C, with an optimum at 70 degrees C; and maximum activity was at pH 7.0. The enzyme was purified using 80% ammonium sulfate precipitation, dialysis, Sephadex G-100 gel filtration, and DEAE-cellulose column chromatography, with a 46-fold and 65% recovery and showed a MW of 63kDa by SDS-PAGE. It was determined that the purified enzyme was stable at 50 and 60 degrees C, and pH 7.0. It was determined that the purified enzyme was stable at 50 and 60 degrees C at the end of 2h. The enzyme retained 100% activity pH 7.0 at the end of 3h. The enzyme was activated by Ca2+, Mn2+, and Triton X-100, but strongly inhibited by Cu2+, Zn2+, Fe2+, and Hg2+. The enzyme follows Michaelis-Menten kinetics with K-m and V-max values of 0.051mM and 1.424mol/min, respectively.Öğe Topraktan izole edilen Streptomyces sp.’den ksilanaz üretimi ve karakterizasyonu(Iğdır Üniversitesi Fen Bilimleri Enstitüsü, 2017) Enez, Barış; Fincan, Sema AgüloğluBu çalışmada topraktan izole edilen Streptomyces sp.'nin izolasyonu, tanımlanması ve optimizasyonu gerçekleştirilmiştir. Streptomyces sp.'nin optimum şartları belirlenerek optimum 35 oC, pH 7.0 ve 52. saat olarak maksimum üreme gerçekleştirdiği tespit edilmiştir. Ksilanaz üretiminin en iyi olduğu koşullar ise 35 oC, pH 7.0 ve 72. saat olarak belirlenmiş ve en iyi enzim aktivitesine 40oC ve pH 7.0'de ulaşılmıştır. Enzim aktivitesi üzerine metallerin etkisi araştırıldığında Zn 2+, Hg 2+ ve Fe 2+ elementlerinin güçlü bir şekilde enzim aktivitesini inhibe ettiği gözlemlenmiştir. Kullanılan deterjanlardan Triton X-100 aktiviteyi arttırırken SDS ise güçlü şekilde inhibe ettiği tespit edilmiş ve enzim aktivitesinin; 35oC-45oC aralıklarında da 1 saat boyunca stabil kaldığı, pH 6.0, ve 7.0 de 1 saat sonunda %100 korunduğu görülmüştür.
