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In this study two different strategy were followed to obtain a D-fructose-oleic acid ester. One of the strategies has been well established enzymatic synthesis of an ester bond. The other strategy excluded the biocatalyst and only used a mixture of two organic solvents as the reaction media, 2-methyl-2-butanol / dimethyl sulfoxide or tert-butanol / dimethyl sulfoxide for the production of D-fructose-oleic acid ester. Ester products obtained were characterised by using FT-IR, NMR, by MS. Product yield was also assessed by HPLC. Results of structural analyses and yield measurement indicated that two approaches produced almost identical ester products.

WOS: 000315167100021, Poly[(maleic anhydride)-co-(vinyl acetate)] (MAVA) copolymer was synthesized by free radical polymerization reaction, in methyl ethyl ketone at 80 degrees C, using benzoyl peroxide as the initiator. The copolymer was then modified with a biomolecule, noradrenaline (NA). The modification reaction was performed at 70 degrees C in dimethylformamide containing triethylamine as the catalyst. The modified polymer was named MAVA/NA. Structural characterization of the copolymer and the modified product was carried out by Fourier transform infrared (FTIR) and 1H NMR and 13C NMR spectroscopy. The FTIR, 1H NMR and 13C NMR spectra confirmed that NA was successfully covalently bound to the MAVA copolymer backbone. Surface morphology was visualized by atomic force microscopy. The cumulative release of NA from MAVA/NA was determined in phosphate buffered saline solution for 7 days at 37 degrees C and compared with MAVA. Cytotoxicity of the MAVA/NA was evaluated by using a mouse fibroblast cell line (L929). Results obtained indicated that MAVA/NA had almost no toxicity and no negative effect on cell viability at 250 mu g mL1 concentration. (c) 2012 Society of Chemical Industry, Science Research Projects Foundation of Cumhuriyet University [F258], This work was supported by the Science Research Projects Foundation of Cumhuriyet University (Project F258).

WOS: 000319496400007, PubMed ID: 23713427, Poly(maleic anhydride-co-styrene) (MAST) was synthesized by a free-radical polymerization reaction. A bioactive molecule, procainamide hydrochloride (PH), was then conjugated to MAST. The conjugation product was named as MAST/PH. Structural characterization of MAST and MAST/PH was carried out by Fourier Transform Infrared and Nuclear Magnetic Resonance spectroscopy. Their molecular weights were determined by size-exclusion chromatography. A mechanism was then suggested for the conjugation reaction. The results of the cytotoxicity assay, employing a mouse fibroblast cell line (L929), indicated that MAST/PH had no cytotoxicity at concentrations 62gmL(1) (p>0.05). Antiproliferative activities of MAST/PH and PH were determined by the BrdU cell proliferation ELISA assay, using C6 and HeLa cell lines. In the experiment, two anticancer chemotherapy drugs, cisplatin and 5-fluorouracil, were included as positive control. Antiproliferative activity results demonstrated that MAST/PH yielded the highest suppression profile (approximately 42%) at 20g/ml, while free PH exerted the same activity at 100g/ml. Interestingly, both MAST/PH and PH suppressed the proliferation of only one of the cell lines, C6 cells. Both cisplatin and 5-fluorouracil yielded approximately 60% antiproliferative activity on C6 cells at 20 and 100g/ml concentrations. Antiangiogenic capacity of both MAST and MAST/PH was also investigated by using the chicken chorioallantoic membrane assay. Results obtained indicated that while MAST/PH could be included into the category of good antiangiogenic substances, the activity score of MAST was within the weak category., Sciences Research Projects Foundation of Cumhuriyet University [F258], This work was supported by Sciences Research Projects Foundation of Cumhuriyet University (Project No: F258). The structural characterizations were carried out at Technology Research and Developing Centre, Erciyes University, Kayseri, Turkey.

WOS: 000390621900011, PubMed ID: 27717786, A thermostable metalloprotease, produced from an environmental strain of Candida kefyr 41 PSB, was purified 16 fold with a 60% yield by cold ethanol precipitation and affinity chromatography (bentoniteacrylamide-cysteine microcomposite). The purified enzyme appeared as a single protein band at 43 kDa. Its optimum pH and temperature points were found to be 7.0 and 105 degrees C, respectively. K-m and V-max values of the enzyme were determined to be 3.5 mg/mL and 4.4 mu mol mL(-1) min(-1), 1.65 mg/mL and 6.1 mu mol mL(-1) min(-1), using casein and gelatine as the substrates, respectively. The activity was inhibited by using ethylenediamine tetraacetic acid (EDTA), indicating that the enzyme was a metalloprotease. Stability of the enzyme was investigated by using thermodynamic and kinetic parameters. The thermal inactivation profile of the enzyme conformed to the first order kinetics. The half life of the enzyme at 95, 105, 115, 125 and 135 degrees C was 1310, 610, 220, 150, and 86 min, respectively. (C) 2016 Elsevier B.V. All rights reserved., Cumhuriyet University (CUBAP) [F-368], This work was supported by The Research Fund of Cumhuriyet University (CUBAP, Project no: F-368).

WOS: 000389090900024, PubMed ID: 27581558, A strain of Lactobacillus fermentum producing two isozymes of a 20 kDa beta-amylase was isolated from the faecal sample of a newborn. The starin was identified by sequencing its 16S rRNA gene. The two beta-amylase isozymes were resolved and visualized by two dimensional protein gel electrophoresis (2-D gel electrophoresis). Some of the physical and biochemical properties of the enzymes were characterized. The beta-amylase displayed two optimum pH s, 5.0 and 10.0 and two optimum temperatures, 45 degrees C and 37 degrees C, respectively. The isozymes hydrolyzed different substrates: glycogen at pH 5.0, and corn starch at pH 10.0. The activity did not require Ca2+, though the activity at pH 10.0 was enhanced in the presence of 5.0 mM and 10.0 mM CaCl2, 110% and 130%, respectively. (C) 2016 Elsevier B.V. All rights reserved., Cumhuriyet University, Turkey/Sivas (CUBAP) [F-408], This work was supported by The Research Fund of Cumhuriyet University, Turkey/Sivas (CUBAP, project number F-408).

WOS: 000294772400076, Maleic anhydride copolymer was modified with another biologically active agent, noradrenaline (NA), using both chemical and enzymatic methods. The modification and synthesized products were named as follows: chemical modification, MASTNAc; enzymatic modification, MASTNAe; enzymatically synthesized MASTNA from individual monomers, MASTNAem. Chemical and enzymatic reactions were performed at 70 degrees C and 38 degrees C, respectively. In the chemical reactions azobisisobutyronitrile was used as the initiator. In the enzymatic reactions, an extracellular extract, including an enzyme with peroxidase-like activity, was used. All the reactions were performed in an organic medium, methyl ethyl ketone. Structural characterization of the copolymer and modified copolymer were carried out by Fourier transform infrared (FTIR) and nuclear magnetic resonance ((1)H NMR). FTIR and (1)H NMR spectra confirmed that NA was successfully covalently bound onto the MAST copolymer backbone by both chemical and enzymatic methods. Surface morphology of the samples was studied by scanning electron microscopy. Results obtained indicated that chemical and enzymatic addition of NA to MAST backbone yielded products having quite similar physical and chemical properties. On the other hand, MASTNA-modified copolymer synthesized by individual monomers appeared to be different in its chemical structure. Furthermore, enzymatic modification and synthesis appeared to provide a good alternative method because it required much milder conditions such as low temperature, and better product qualities: higher solubility in water, higher yield and purity. (C) 2011 Wiley Periodicals, Inc. J Appl Polym Sci 122: 2821-2828, 2011

WOS: 000318710600009, Three maleic anhydride copolymers were synthesized by free-radical copolymerization. The synthesized products were named as follows: maleic anhydride-styrene (MAST); maleic anhydride-vinyl acetate (MAVA), and maleic anhydride-methyl methacrylate (MAMMA). Initiators used in the reactions were azobisisobutyronitrile (AIBN, 70 A degrees C, benzene) for MAST and benzoyl-peroxide [BPO, 80 A degrees C, methyl ethyl ketone (MEK)] for MAVA and MAMMA. Structural characterizations were carried out by Fourier transform infrared (FTIR) and nuclear magnetic resonance [H-1 NMR, C-13 NMR, and C-13-APT (attached-proton test)] spectrometry. Surface morphology was studied by scanning electron microscopy (SEM). Solubility of the copolymers was examined in water and in twelve different organic solvents. Cytotoxicity of the copolymers and the solvents was evaluated by using a mouse fibroblast cell line (L929), copolymers had almost no toxicity. Of the twelve organic solvents, acetone, MEK, and tetrahydrofuran (THF) produced the least toxicity. MEK was found to be the best solvent and used for the solvation of the copolymers., Sciences Research Projets Foundation of Cumhuriyet University [F258], This study was supported by Sciences Research Projets Foundation of Cumhuriyet University (Project No.: F258).

WOS: 000304230000016, PubMed ID: 22387519, A Thermoalkalophilic amylase was produced from an environmental bacterial isolate. The enzyme was then immobilized through its amino groups onto the epoxy rings of magnetic poly glycidyl methacrylate [m-poly (GMA)] beads. The free enzyme was active within a large pH range, between 7 and 12 and displayed the optimum activity at 95 degrees C and pH 10. The immobilization appeared to increase the stability of the enzyme as its bound form showed optimum activity at 105 degrees C and pH 11.0. Kinetic studies demonstrated that immobilized enzyme had higher K-m and lower V-max values. The activity of the free and bound enzyme was determined, at 37 degrees C and pH 10.0 and pH 11.0, respectively, in the presence of various organic solvents and detergents (5%, v/v). Results obtained indicated that detergents, sodium dodecyl sulfate (SDS) and TritonX-100, caused six fold increase and that various organic solvents also increased the activity of the amylase. (C) 2012 Elsevier B.V. All rights reserved.

WOS: 000281303100022, 16S rRNA gene was amplified from faecal or milk total genomic DNA of eight women by polymerase chain reactions (PCR) using a pair of bacteria specific universal oligonucleotide primers. Amplification products were digested with both HaeIII and TaqI restriction enzymes. Sampling period covered the second and third trimester of pregnancy and further 6 months after birth for the collection of breast milk. Digestion products were resolved in an 8% polyacrylamide gel and restriction fragment length polymorphism (RFLP) profiles were visualized by silver staining. A control group was also prepared from eight other women who were single and without children. In the RFLP profiles, clearly discernible 66 digestion products (bands) were selected and subjected to unweighted pair-group method with arithmetic mean analysis (UPGMA). Results indicated that almost 58% of the clustering comprised common banding patterns, shared by faecal, milk and control samples. Nine of the clusters (approximately 13%) were exclusive to faecal and milk samples. Prominent bands present in the milk RFLP patterns indicated that four of the mothers who adopted traditional food sources could have almost identical prominent bacteria in their milk., CUBAP (The Scientific Research Projects Council of Cumhuriyet University) [F-168], This work was supported by CUBAP (The Scientific Research Projects Council of Cumhuriyet University) with the project number F-168.

WOS: 000337768400008, Streptococcus thermophilus is a commonly used starter bacterium in dairy industry. It reduces the pH of milk rapidly and equilibrates the medium for the growth of Lactobacillus delbrueckii subsp. bulgaricus during yoghurt fermentation. Efforts to increase the diversity of artisanal yoghurt starters are not only important to bring new strains with novel and desirable characteristics, but also for the preservation of natural diversity which diminishes with the overuse and spread of industrial starters to natural resources. In the present study, 14 artisanal yoghurt samples were processed for the isolation of promising strains for yoghurt starter culture production and 66 strains were subsequently characterized. They were all identified as S. thermophilus using species-specific PCR and 16S rRNA gene sequencing. Genotypic diversity at the strain level was investigated by pulsed field gel electrophoresis (PFGE), and 22 homology groups were obtained. Further phenotypic characterization unearthed a significant phenotypic heterogeneity within homology groups, mostly with atypical novel character. Only 7 out of 66 strains showed S. thermophilus type-strain like phenotypic traits. Majority of the isolates were determined to be protease positive and fast milk acidifier to be used as yoghurt starter culture. (C) 2013 Elsevier Ltd. All rights reserved., Government Planning Institution under the project "The Production of Cheese and Yoghurt Starter Cultures and Lactase Enzyme for the Dairy Industry: Traditional and Modern Solutions against Lactose Intolerance", We would like to acknowledge Mert Sudagidan for his scientific assistance during the PFGE study, Elif Sinem Celik for her contribution to the bacterial isolation and further flavor profiling of co-culture growths in her thesis study, Elcin Soydemir for the phage sensitivity tests of the isolates in her thesis study, and Hatice Yavuzdurmaz for her contribution to the bacterial isolation. This study was supported by the Government Planning Institution under the project "The Production of Cheese and Yoghurt Starter Cultures and Lactase Enzyme for the Dairy Industry: Traditional and Modern Solutions against Lactose Intolerance". Prof. Dr. Nihat AKIN is acknowledged for kindly providing yogurt samples that was used for the isolation of microbial species.

WOS: 000252496100020, PubMed ID: 17927757, Aims: To isolate Bacillus thuringiensis strains from different olive-related habitats (olive groves and olive oil factories) in Turkey and to characterize these strains by molecular methods. Methods and results: A total of 150 samples, consisting of olive grove soil, green olive leaves, olive leaf residues, animal faeces, olive pomace and dust, were examined for the presence of B. thuringiensis. One hundred B. thuringiensis strains were isolated from 54 environmental samples (36%) and characterized in terms of crystal morphology, cry and cyt gene content by polymerase chain reaction, plasmid profiles and 16S-internal transcribed spacer ribosomal DNA restriction fragment length polymorphism (16S-ITS rDNA RFLP). The highest percentage of samples containing B. thuringiensis was found in 38 out of 54 total soil samples (70%). Of the 100 B. thuringiensis isolates, the most frequent crystal shapes were irregularly shaped (24%), spherical-irregular pointed (19%), cuboidal (17%) and spherical (16%). The cry1 plus cry4 genotype was the most abundant genotype in our collection (21%). RFLP analysis of the amplified 16S-ITS rDNA revealed 11 distinct patterns for the isolates and 10 reference strains. Conclusions: Bacillus thuringiensis isolates showed a great genetic diversity and crystal shape heterogeneity. Significance and Impact of the Study: This is the first study on the isolation and characterization of B. thuringiensis from olive-related habitats in Turkey. No correlation was observed between the cry genotypes and insecticidal crystal shapes of the isolates. Restriction profiles of 23% of the isolates were found to be different from those of the 10 reference strains used.