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  • Küçük Resim
    Öğe
    Diyadin (Ağrı) sıcak su kaynaklarından bakteri izolasyonu ve bazı enzimleri üzerinde çalışmalar
    (2017) Matpan, Fatma; Güven, Kemal
    Bu çalışmada, Diyadin (Ağrı) sıcak su kaynaklarından su ve toprak örnekleri alınarak bu örneklerden 4 bakteri izole edildi. Bu izolatların morfolojik, fizyolojik ve biyokimyasal analizleri yapıldı. İzole edilen bakterilerden 1 nolu bakterinin çubuk şeklinde, gram pozitif, spor oluşturan, hareketli, ılımlı termofil olduğu ve 3 nolu bakterinin ise çubuk şeklinde, gram pozitif, spor oluşturan, hareketsiz ve ılımlı termofil olduğu belirlendi. Bakterilerin üremesi için optimum pH 1 ve 3 nolu izolatlar için sırasıyla 8 ve 7, optimum üreme sıcaklığı ise sırasıyla 50 oC ve 55 o C olarak belirlendi. Elde edilen izolatların ekstraselüler ?–amilaz ve proteaz enzimi üretme yetenekleri araştırılarak, enzim aktivasyonunun optimum koşulları belirlendi. 1 nolu izolatın optimum ?–amilaz üretimini 40. saatte (21,96 U/mg) gerçekleştirdiği ve ?– amilaz aktivitesinin optimum pH ve sıcaklık değerlerinin sırasıyla 8 ve 60 oC olduğu, proteaz üretiminin optimum 24. saatte (771 U/mg) gerçekleştiği ve proteaz aktivitesinin optimum pH ve sıcaklık değerlerinin sırasıyla 9 ve 50 oC olduğu belirlendi. 3 nolu izolat için ise ?–amilaz üretiminin optimum 24. saatte (32 U/mg) gerçekleştiği ve amilaz aktivitesinin optimum pH ve sıcaklık koşullarının 7 ve 70 oC olduğu, protez üretiminin optimum 36. saatte (421 U/mg) gerçekleştiği ve proteaz aktivitesinin optimum pH ve sıcaklığının sırasıyla 10 ve 50 oC olduğu tespit edildi. Bu izolatlardan elde edilen ?–amilaz ve proteaz enzimleri amonyum sülfat çöktürmesi ve diyaliz işlemlerine tabi tutuldu ve bu enzimlerin aktivitesi üzerine ağır metallerin etkisi araştırıldı. 1 (KP1)’in ekstraselülar ?-amilaz aktivitesinin 1,5 mM Mn+2 ve 1,5 mM Cu+2 iyonlarının bulunduğu ortamda arttığı, %1’lik SDS bulunan ortamda aktivitenin azaldığı, 1,5 mM Hg+2 iyonu bulunan ortamda ise enzimin tamamen inhibe olduğu belirlendi. İzolat 3 (DV3)’ün ?–amilaz aktivitesinin 1,5 mM Hg+2 iyonu bulunan ortamda tamamen inhibe olduğu tespit edildi. İzolat 1 (KP1) için proteaz aktivitesinin 1,5 mM Ca+2 ve 1,5 mM Cu+2 iyonlarının bulunduğu ortamda arttığı, 1,5 mM Hg+2 iyonu 1,5 mM EDTA, %1’lik SDS bulunan ortamda aktivitenin azaldığı ve 1,5 mM PMSF bulunan ortamda ise enzimin tamamen inhibe olduğu belirlendi. İzolat 3 (DV3) için 1,5 mM Ca+2 ve 1,5 mM Zn+2 iyonlarının bulunduğu ortamda proteaz aktivitesinin arttığı, 1,5 mM Hg+2, %1’lik SDS bulunan ortamda ise aktivitenin azaldığı, 1,5 mM EDTA, 1,5 mM PMSF bulunan ortamda ise enzimin tamamen inhibe olduğu tespit edildi. Anahtar Kelimeler: Sıcak su kaynakları, Bakteri izolasyonu, Termofil bakteri, Basil, ?-Amilaz, Proteaz, Ağır metal
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    Öğe
    Effects of Various Inhibitors on ?-galactosidase Purified from the Thermoacidophilic Alicyclobacillus acidocaldarius Subsp Rittmannii Isolated from Antarctica
    (Korean Soc Biotechnology & Bioengineering, 2011) Guven, Reyhan Gul; Kaplan, Alevcan; Guven, Kemal; Matpan, Fatma; Dogru, Mehmet
    beta-Galactosidase purified from the thermoacidophilic Alicyclobacillus acidocaldarius subsp. rittmannii isolated from Antarctica is a member of the GH42 family. The enzyme was not effected by various concentrations of its reaction product glucose, but was greatly inhibited by the other reaction product galactose using both substrates, ONPG and lactose. Linewever-Burk plot analysis derived from both ONPG and lactose hydrolysis results showed that galactose is a mixed-type inhibitor of the purified beta-galactosidase. The enzyme was slightly activated by Mg(2+) (13% at 20 mM), while inhibited at higher concentrations of Ca(+2) (33% at 10 mM), Zn(+2) (86% at 8 mM) and Cu(+2) (87% at 4 mM). The enzyme activity was not significantly altered by the metal ion chelators EDTA and 1,10-phenanthroline up to 20 mM, indicating that this enzyme is not a metalloenzyme. 2-Mercaptoethanol and DTT were found to enhance beta-galactosidase activity, while p-chloromercuribenzoic acid (PCMB) completely inhibited enzymatic activity (97% at 1 mM; 99.7% at 2 mM), indicating at least one essential Cys residue modified by the reagents in the active site of beta-galactosidase. Iodoacetamide and N-ethylmaleimide had little effect on the beta-galactosidase. Phenylmethylsulfonyl fluoride (PMSF) inhibited the enzyme strongly (19.8% at 1 mM; 71.9% at 10 mM), also showing the participation of serine for enzyme activity.
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    Öğe
    Geobacillus subterraneus subsp aromaticivorans subsp nov., a novel thermophilic and alkaliphilic bacterium isolated from a hot spring in Sirnak, Turkey
    (Microbiol Res Foundation, 2012) Poli, Annarita; Guven, Kemal; Romano, Ida; Pirinccioglu, Hamsi; Guven, Reyhan Gul; Euzeby, Jean Paul Marie; Matpan, Fatma
    A new thermophilic spore-forming strain Ge1(T) was isolated from the Guclukonak hot spring in Sirnak, Turkey. The strain was identified by using a polyphasic taxonomic approach. Strain Ge1(T) was Gram-positive, spore-forming, alkaliphilic rod-shaped, motile, occurring in pairs or filamentous. Growth was observed between 30 and 65 degrees C (optimum 60 degrees C) and at pH 5.5-10.0 (optimum pH 9.0). It was capable of utilizing starch, growth was observed at 0-3% NaCl (w/v) and was positive for catalase and urease. The major cellular fatty acids were iso-C-15:0 and iso-C-17:0, and the predominant lipoquinone found was menaquinone MK7 type. The DNA G+C content of the genomic DNA of strain Ge1(T) was 52.0%. Comparative 16S rRNA gene sequence studies showed that the isolate belonged to the genus Geobacillus. The DNA-DNA hybridization mean values between the representative strain Ge1(T) and the closely related species G. subterraneus, G. thermodenitrificans, G. thermocatenulatus, G. vulcani and G. thermoleovorans were 69.3%, 57%, 37%, 27% and 26%, respectively. The results of DNA-DNA hybridization, physiological and biochemical tests allowed genotypic and phenotypic differentiation of strain Ge1(T). Based on these results, we propose assigning a novel subspecies of Geobacillus subterraneus, to be named as Geobacillus subterraneus subsp. aromaticivorans subsp. nov. with the type strain Ge1(T) (DSM 23066 (T)= CIP 110341(T)).
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    Öğe
    Isolation of a thermophilic Anoxybacillus flavithermus sp nov and production of thermostable ?-amylase under solid-state fermentation (SSF)
    (Bmc, 2012) Ozdemir, Sadin; Matpan, Fatma; Okumus, Veysi; Dundar, Abdurrahman; Ulutas, Mehmet Sefa; Kumru, Mert
    A new bacteria was isolated from hot-spring water of Gazligol, Afyonkarahisar in Turkey. Based on morphological and biochemical tests and 16S rRNA gene sequence analysis, the isolate belonged to the Anoxybacillus flavithermus species which has 99% similarity with the bacterium DNA. The production of alpha-amylase by thermophilic Anoxybacillus flavithermus was investigated under solid-state fermentation by using some agricultural waste as substrates. Solid substrates such as rice husk, banana husk, millet, water melon husk, lentil bran, wheat bran and maize oil cake were studied for enzyme production. Of these, rice husk was proved as the best substrate for alpha-amylase production (1,271 U/mg). The maximum alpha-amylase production was observed as 1,803 U/mg at 72 h, 1,000 mu m particle size, 70% initial moisture content (w/v), and 40% inoculum level (v/w). Among the various nitrogen sources tested, 1% peptone (3,170 U/mg) was found to be the best nitrogen source for alpha-amylase production. As additional carbon sources, 1% starch (2,364 U/mg) enhanced alpha-amylase production. The optimum temperature for the activity of alpha-amylase was found to be 70A degrees C. The enzyme was optimally active at pH 6.0 and stable in the pH range of 6.0-8.0.
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    Öğe
    PRODUCTION AND CHARACTERIZATION OF PARTIALLY PURIFIED EXTRACELLULAR THERMOSTABLE ?-AMYLASE BY Bacillus subtilis IN SUBMERGED FERMENTATION (SmF)
    (Taylor & Francis Inc, 2011) Ozdemir, Sadin; Matpan, Fatma; Guven, Kemal; Baysal, Zubeyde
    A Bacillus strain was isolated from soil samples from the campus area of Dicle University. Based on 16S ribosomal RNA sequencing, the microorganism was closely related to Bacillus subtilis. Effects of different culture medium, incubation time, carbon and nitrogen sources, and various starches, flours, and chemicals on alpha-amylase production were examined. Maximum enzyme production (7516 U/mL) was obtained in a basal medium A containing 0.05% Tween 40 in 24 h. Partially purified enzyme showed maximum activity at 60 degrees C with an optimum pH of 6.0. The effects of 0.2% detergents (sodium dodecyl sulfate [SDS], CHAPS [3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate], and commercial detergent Omo Matic) on partially purified enzyme activity over a period of time (15-150 min) were examined and the order of inhibition effect from the most to the least was found as SDS> Omo Matic> CHAPS. Different metal ions inhibited alpha-amylase activity at low concentrations (1.5 mM). Co2+ was a mild inhibitor and Hg2+ and Cd2+ were potent inhibitors, whereas Ca2+ and Mg2+ increased the enzyme activity. At 20 mM, Ca2+ enhanced enzyme activity, and different Ca2+ concentrations (10-300 mM) were studied.