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  • MakaleAçık Erişim2024
    Characterization of cellulose produced by bacteria isolated from different vinegars

    Güzel, Melih

    Traditional vinegars are naturally produced from sugar- or starch-containing raw materials, through alcoholic fermentation followed by acetic fermentation. Fermentation is a spontaneous and complex process involving interactions between various microorganisms. In this study, we produced vinegar using traditional methods from six fruits: rosehip, pear, fig, wild pear, apple, and plum. Bacteria that produce bacterial cellulose (BC) were isolated from these vinegars and identified. In addition, we investigated the properties of BC produced from these bacteria. The strains isolated from vinegars were identified as Gluconobacter oxydans strain MG2022, Acetobacter tropicalis strain MG2022, Acetobacter fabarum strain MG2022, Komagataeibacter saccharivorans strain MG2022, K. saccharivorans strain EG2022, and Acetobacter lovaniensis strain OD2022. In total, 0.83–2.04 g/L BC was produced and the bacterial strain isolated from pear vinegar yielded the most BC. BC produced by the bacterial strain isolated from wild pear vinegar had the highest thermal stability and crystallinity (87.44 %). Overall, this study shows that different fruits contain different BC-producing bacteria in their natural flora and vinegars obtained from fruits can be used in BC production. Also, different BC-producing bacteria can be isolated from different vinegars, and BC produced by these bacteria might have different properties.

    • SDG 2 · Açlığa Son
    • SDG 12 · Sorumlu Üretim ve Tüketim
  • MakaleYalnız künye2020
    Preparation and characterization of bacterial cellulose produced from fruit and vegetable peels by Komagataeibacter hansenii GA2016

    Güzel, Melih; Akpınar, Özlem

    This study focused on the investigation of bacterial cellulose production potency of some fruit and vegetable peels (cucumber, melon, kiwifruit, tomato, apple, quince and pomegranate) with Komagataeibacter hansenii GA2016. Fruit and vegetable peels were hydrolyzed, used for bacterial cellulose (BC) production and their chemical, physical, thermal and structural features were compared to BC from Hestrin–Schramm medium (HSBC) and plant cellulose (CP). Except for pomegranate peel hydrolysate, all the fruit and vegetable peel hydrolysates supplied to K. hansenii GA2016 supported the BC production. Among the fruit and vegetable peel hydrolysates, the highest BC production was observed in kiwifruit peel hydrolysate (11.53%), while the lowest production was observed in apple peel hydrolysate (1.54%). Water-holding capacities of the BCs were ranged from 627.50% to 928.79% and higher than HSBC (609.30%), average fiber diameters were ranged from 47.64 nm to 61.11 nm and thinner than HSBC (74.29) and CP (10,420 nm), crystallinities were ranged from 80.27% to 92.96%, thermal capacities BCs were higher than HSBC and CP. For the BC productions, utilization of the fruit and vegetable peels as the sole nutrient source could reduce the production costs and among the polysaccharides, increase the use of BC in industry.

    • SDG 2 · Açlığa Son
    • SDG 12 · Sorumlu Üretim ve Tüketim
  • MakaleYalnız künye2019
    A novel endo-β-1,4-xylanase from Pediococcus acidilactici GC25; purification, characterization and application in clarification of fruit juices

    Adiguzel, Gulsah; Faiz, Ozlem; Sisecioglu, Melda; Sari, Bilge; Baltaci, Ozkan; Akbulut, Sumeyya; Genc, Berna; Adiguzel, Ahmet

    A novel extracellular xylanase was purified and characterized from Pediococcus acidilactici GC25 (GenBank number: MF289522). The purification was 4.6-fold with a yield of 43.61% through acetone precipitation, Q-Sepharose, and CM-Sepharose ion change chromatography. The molecular weight of the enzyme was 48.15 kDa, and the optimum pH and temperature were 7.0 and 40 °C, respectively. The maximum activity was observed between 20 and 50 °C. Although it was active within a wide pH range (pH 2.0–9.0), it retained over 85% of its activity after 24 h incubation; and over 70% of its activity after 168 h incubation in neutral and alkaline pH. It was observed that the enzyme showed high stability with K+, Ba2+, Cd2+, Co2+, Sr2+, Mg2+, Ca2+, Al3+, Zn2+, and Ni2+ ions. The Km and Vmax for the xylanase were 3.10 mg mL−1 and 4.66 U/mg protein, respectively. It was determined that treatment of different fruit juices with P. acidilactici GC25 xylanase improved the clarification. The highest increase in the reducing sugar amount and decrease in the turbidity was 24.47 ± 1.08 and 21.22 ± 0.58 for peach juice at 0.15 U/mL enzyme concentration. These results showed that the xylanase purified from P. acidilactici GC25 may have a wide potential in biotechnological processes of the food and baking industry.

    • SDG 12 · Sorumlu Üretim ve Tüketim
  • MakaleYalnız künye2018
    New xylanolytic enzyme from Geobacillus galactosidasius BS61 from a geothermal resource in Turkey

    Sari, Bilge; Faiz, Ozlem; Genc, Berna; Sisecioglu, Melda; Adiguzel, Ahmet; Adiguzel, Gulsah

    In this study, isolation, conventional and molecular characterizations of ten thermophilic bacteria from Rize/Ayder were carried out. Xylanase from Geobacillus galactosidasius BS61 (GenBank number: KX447660) was purified by acetone precipitation, Diethylaminoethyl-cellulose and Sephadex G-100 chromatographies. The xylanase of G. galactosidasius BS61 in clarifying fruit juice was also investigated. Enzyme was purified 29.80-fold with 75.18% yield; and molecular weight was determined as 78.15 kDa. The optimum temperature of xylanase was 60 °C. The enzyme activity was maintained fully after 24 h and over 50% after 168 h at pH 4.0–10.0, while optimum pH was 7.0. Km and Vmax for beech wood xylan were measured as 3.18 mg mL−1, 123 U mg protein−1. In addition, Ca2+, Na+, Al3+, Zn2+, Cd2+, Mg2+, Ni2+, Cu2+ had decreasing effect on enzyme activity, while enzyme activity had been protected against anions, especially HSO3− and HPO4 2− stimulated enzyme activity. Xylanase applications (with 15 U/mL enzyme activity) in orange and pomegranate juices were increased; and the sugar and turbidity amounts were reduced 17.36% ± 1.18 and 30.52 ± 1.23, respectively. These results indicated that the xylanase of G. galactosidasius BS61 has biotechnological potential in juice clarification due to its stability against metal ions, chemicals and high pH-values.

  • MakaleAçık Erişim2018
    A study of Bos taurus muscle specific enolase; biochemical characterization, homology modelling and investigation of molecular interaction using molecular docking and dynamics simulations

    Sariyer, Emrah; Yakarsonmez, Sinem; Danis, Ozkan; Turgut-Balik, Dilek

    Tropical theileriosis caused by Theileria annulata obligate parasite that infect ruminant animals, including Bos taurus. The disease results massive economic losses in livestock production worldwide. Here we describe cloning, expression and both biochemical and structural characterization of beta enolase from Bos taurus in vitro and in silico. The interconversion of 2‑phosphoglycerate to phosphoenolpyruvate was catalyzed by enolase is a metalloenzyme in glycolytic pathway and gluconeogenesis. Enolase from Bos taurus was cloned, expressed and the protein was purified at 95% purity using cobalt column by affinity chromatography. The optimum enzymatic activity was calculated at pH 6.5. For the first time in the literature, the kinetic parameters of the enzyme, Vmax and Km, were measured as 0.1141 mM/min and 0.514 mM, respectively. Besides, Bos taurus enolase 3-dimensional structure was built by homology modelling to be used in silico analyses. The interactions of the enzyme-substrate complex were elucidated by molecular dynamics simulations for 100 ns. These interactions were found to be the same as experimentally determined interactions in yeast. These results would enable further structure based drug design studies with the biochemical characterization of the host organism Bos taurus enolase enzyme in vitro and the elucidation of behavior of enzyme-substrate complex in silico.

  • MakaleAçık Erişim2017
    Novel eugenol derivatives: Potent acetylcholinesterase and carbonic anhydrase inhibitors

    Topal, Fevzi; Gulcin, Ilhami; Dastan, Arif; Guney, Murat

    Eugenol was used as starting material to obtain some phenolic compounds. The synthesis of these phenolic compounds was performed in a two-step procedure. The structures of the formed products (novel eugenol derivatives 1–6) have been determined on the basis of NMR spectroscopy and other spectroscopic methods. The compounds were tested in terms of carbonic anhydrase (CA) inhibition potency. Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes, which catalyse the reaction between carbon dioxide (CO2) and water (H2O), to generate bicarbonate (HCO3−) and protons (H+). CO2, HCO3− and H+ are essential molecules and ions for many important physiologic processes occurring in all living organisms. Acetylcholinesterase (AChE, E.C.3.1.1.7) is found in high concentrations in the red blood cells and brain. Novel eugenol derivatives (1–6) were tested for the inhibition of two cytosolic CA isoforms I, and II (hCA I, and II) and AChE. These compounds demonstrated effective inhibitory profiles with Ki values in ranging of 113.48-738.69 nM against hCA I, 92.35-530.81 nM against hCA II, and 90.10-379.57 nM against AChE, respectively. On the other hand, acetazolamide clinically used as CA inhibitor, shoed Ki value of 594.11 nM against hCA I, and 120.68 nM against hCA II, respectively. Also, AChE was inhibited by tacrine as an AChE inhibitor at the 71.18 nM level.

    • SDG 3 · Sağlık ve Kaliteli Yaşam
Tam Kayıt
AlanDeğerDil
creativeworkseries.issn0141-8130
dc.date.accessioned2026-10-22T10:21:24.909978339Z
dc.date.available2026-10-22T10:21:24.909978339Z
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/gumushane/13481
dc.publisherElsevier B.V.
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleInternational Journal of Biological Macromolecules
dspace.entity.typeJournal