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Öğe Ankaferd Blood Stopper with antibiofilm potential successfully inhibits the extracellular matrix degradation enzymes and promotes wound healing of 3T3 fibroblasts in vitro(Tubitak Scientific & Technical Research Council Turkey, 2018) Boran, Rukiye; Baygar, Tuba; Saraç, Nurdan; Uğur, AyselBackground/aim: The potential inhibitory effects of Ankaferd Blood Stopper (ABS) against biofilm formation of oral microorganisms and its capacity for collagenase, hyaluronidase, and elastase inhibitions that have important roles in wound healing have been investigated. Materials and methods: The wound healing potential was determined by its inhibition ability on collagenase, hyaluronidase, and elastase enzyme activities and was evaluated via scratch wound healing assay on murine 3T3 fibroblasts. The antibiofilm activity was tested against eight oral microorganisms using the crystal violet staining method. Results: At 10% ABS successfully inhibited the biofilm formation of the tested microorganisms. Enzyme inhibition analysis revealed that 3% ABS significantly inhibited all three enzymes related to wound healing. The scratch assay showed that wound closure was faster than that of the control for the 3% ABS/plate. Conclusion: The findings of the present study indicated that ABS has effective wound healing potential with its strong antibiofilm activity against oral cavity microorganisms.Öğe Antimicrobial, antifibrinolytic, enzyme inhibitory and wound healing properties of zinc borate(TENMAK Bor Araştırma Enstitüsü, 2023) Boran, Rukiye; Baygar, Tuba; Saraç, Nurdan; Ayrıkçıl, Semih; Yılmaz, Derviş; Uğur, AyselBoron containing compounds (BCGs) have recently been used for pharmaceutical applications. Zinc, an essential element, is known to be one of the most promising biodegradable metals. The present study was conducted to determine the wound healing properties of zinc borate with its antimicrobial, antifibrinolytic and enzyme inhibitory characteristics. In vitro scratch wound healing assay revealed that zinc borate at 0.01 µg/mL concentration stimulated the proliferation of 3T3 fibroblast cells after 24 h of scar formation. The highest enzyme inhibition was observed against collagenase at 1 mg/mL (81.5%). Minimum inhibition concentration (MIC) values were determined as 1 mg/mL and 0.5 mg/mL against Candida albicans and Staphylococcus aureus, respectively. Zinc borate did not have any fibrinolytic activity at 1, 0.5 and 0.1 mg/mL concentrations. It can be suggested that zinc borate can be used effectively to improve the wound healing process and to prevent the possible wound infections.Öğe Burkholderia multivorans SB6 lipase as a detergent ingredient: characterization and stabilization(SPRINGER HEIDELBERG, 2016) Boran, Rukiye; Uğur, AyselIn this study, 265 bacterial isolates were collected from kitchen wastewater samples using Rhodamine B agar medium. Of these, 115 isolates were found to respond positively to the addition of commercial detergents. Using 16S rRNA sequence analysis, the isolate demonstrating the high stability towards commercial detergents was identified as Burkholderia multivorans. An SB6 lipase with a molecular mass of 70 kDa was purified from B. multivorans. The purified enzyme showed optimal activity at pH 9.0 and 40 A degrees C and remained stable in the presence of various metal ions, surfactants, and oxidizing agents. The addition of boron compounds improved the pH stability and thermostability of the enzyme, which displayed stability against some commercial detergents; moreover, this stability increased when boron compounds were added to the incubation medium as stabilizers. These properties make SB6 lipase an ideal choice as an additive in detergent formulations.Öğe Characterisation of streptomyces violascens OC125-8 lipase for oily wastewater treatment(Springer, 2019) Boran, Rukiye; Uğur, Aysel; Saraç, Nurdan; Ceylan, ÖzgürIn this study, the lipase-producing bacterium Streptomyces violascens (GenBank number MF621564) was identified, and the extracellular S. violascens OC125-8 lipase produced by this strain was characterised for use in wastewater treatment. The lipase was partially purified by ammonium sulphate precipitation at a final yield of 3.28-fold purification and a recovery of 56%. The S. violascens OC125-8 lipase exhibited optimum catalytic activity at 40 degrees C and pH 8.0; it was stable at 30-40 degrees C with more than 86% residual activity after 1h; it was also stable over a relatively broad pH range of pH 7.0-11.0, retaining 83.3-100% activity. V-max and K-m values were calculated as 0.61 mu mol/min/mg and 0.259mM, respectively. Enzyme activity significantly increased in the presence of Fe2+ ion but was inhibited by Ca2+, Mn2+, Cu2+ and Mg2+. The addition of a serine protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), strongly inhibited enzyme activity while ethylenediaminetetraacetic acid (EDTA), a metal chelating agent, had no inhibitory effect. The enzyme was fairly stable in the presence of surfactants as well as sodium perborate. Examination of commercial detergent tolerance revealed that the lipase was strongly stable in Tursil (88%), Pril (97%) and Fairy (98.5%), while the lipase was activated in Omo (113.4%) and Ariel (128.3%). Moreover, the lipase showed highest activity towards olive oil (100%), sunflower oil (90%) and burned sunflower oil (55%), while corn oil (44%) and burned olive oil (15%) were less hydrolysed by the enzyme. These properties demonstrate that S. violascens OC125-8 lipase is an ideal choice for oily wastewater management.Öğe Detergent compatible extracellular lipase from streptomyces cellulosae AU-10: A green alternative for the detergent industry(Wıley, 2018) Boran, RukiyeEnzymes can decrease the environmental and economic load of detergent products by reducing the amount of chemicals used in detergents and by allowing washing at ambient temperatures. In this study, Streptomyces cellulosae AU-10 (GenBank accession number: MG780240) lipase was purified 7.08-fold with 68% yield using an aqueous 2-phase system. The Streptomyces sp. AU-10 lipase showed maximal activity at pH 9.0 and 40 degrees C. Hundred percent activities were measured in the pH range from 9.0 to 11.0 for 1 h. The enzyme was also highly stable at 30-50 degrees C. The values of K-m and V-max were calculated as 0.34mM and 0.83mMmin(-1), respectively. The lipase has high hydrolytic activity for olive oil and sunflower oil. The effect of ethylenediamine tetraacetic acid on the enzyme has shown that the lipase is a metalloenzyme. The activity increased in the presence of Fe2+, Cu2+, and various boron compounds. The enzyme has shown a good stability not only with surfactants but also with oxidizing agents. In addition, activities in the presence of Omo, Ariel, Tursil, Pril, and Fairy were measured as 108.8%, 115.6%, 98.35%, 140.4%, and 107.6%, respectively. Considering its remarkable ability, the S. cellulosae AU-10 lipase can be considered as a potential additive in the detergent industry.Öğe In vitro biological activities of potassium metaborate; antioxidative, antimicrobial and antibiofilm properties(TENMAK Bor Araştırma Enstitüsü, 2022) Baygar, Tuba; Saraç, Nurdan; Ceylan, Özgür; Uğur, Aysel; Boran, Rukiye; Balcı, UyduAntioxidant, antimicrobial and antibiofilm activities of potassium metaborate (KBO2) was investigated within the present study. Antioxidant capacity of potassium metaborate was determined by ?-carotene bleaching (BCB) assay and hydroxyl radical scavenging activity. Potassium metaborate was evaluated for its antimicrobial effects against selected Gram-positive bacteria, Gram-negative bacteria and a yeast via broth dilution method. The inhibition capability of potassium metaborate on the microbial biofilm formation of tested microorganisms was measured by microplate biofilm method using MTT (3- [4, 5- dimethyl-2-thiazolyl]-2, 5-diphenyl-2H-tetrazolium-bromide). Biofilm inhibition capacity of potassium metaborate was also observed by Scanning Electron Microscope (SEM). Potassium metaborate was found to have the ability to scavenge hydroxyl radicals with an inhibition rate of 71.13% at 100 mM concentration. Antioxidant activity of potassium metaborate as determined by BCB assay gave higher result with an inhibition rate of 86.96% at the same concentration. According to the MIC (minimum inhibition concentration) values, the potassium metaborate inhibited the growth of C. albicans, S. aureus and E. coli at 62.5 mM concentrations while it was 31.25 mM for B. subtilis and 125 mM for P. aeruginosa. The highest antibiofilm activity was determined at the MIC of potassium metaborate with the reduction rate of 90.18% against C. albicans. It was concluded that, potassium metaborate have strong biological activities and can be effectively used for biomedical and environmental solutions.Öğe In vitro evaluation of the effectiveness of different bodipy dyes as photosensitizer in methicillin-resistant staphylococcus aureus treatment(Mugla Sitki Kocman University, 2018) Boran, Rukiye; Pamuk Algı, Melek; Uğur, AyselThe antibiotic period is now ending and the probability of discovering new classes of antibiotics is considerably low. It is required to find out alternative antimicrobial technologies that bacteria will not be able to develop resistance, and that will be equally effective regardless of the current resistance situation. In this regard, we investigated antimicrobial photodynamic inactivation effects of three boradiazaindacenes (BODIPYs) 1?3 against methicillin-resistant Staphylococcus aureus (MRSA). BODIPYs 1?3 with different substituents at the meso position (-NMe2, -NO2 and -Br, respectively) were synthesized. The photodynamic inactivation effects of BODIPYs 1?3 were tested against one broad spectrum antibiotic resistant bacterial modelstrain, a clinically described MRSA. In particular BODIPY 2 wasfound more effective when compared to the others at 25, 50 and 100 nM concentrations. BODIPYs 1?3 did not show any toxic effect in the dark at given concentrations. In addition, a high degree of photodynamic inactivation were detected with 2 and 3 by irradiation at 6.66 ? 8.88 J/cm2 light doses, while the efficiency of 1 was not significantly affected from illumination times. The results indicate that BODIPYs, especially nitro group BODIPY 2, can be used in the photodynamic inactivation of MRSA at nanomolar concentrations and low energy doses.Öğe Investigation of hyaluronidase, collagenase and elastase inhibitory potentials and comparative evaluation of the antimicrobial, antioxidant and homeostatic activities of two natural polysaccharides(Süleyman Demirel Üniversitesi, 2018) Boran, Rukiye; Uğur, Aysel; Saraç, NurdanThe aim of this study was to investigate the hyaluronidase, collagenase and elastase inhibitory effects, which play important role for wound healing, together with the antibacterial, antioxidant and homeostatic activities of tragacanth gum (TG) and locust bean gum (LBG). The antimicrobial activities were tested against four bacteria and the antioxidant activities were estimated by the 1,1-diphenyl-2-picrylhydrazyl (DPPH), hydrogen peroxide (H2O2) radical scavenging and ?-carotene bleaching assays. Homeostatic effect was evaluated with the Prothrombin Time (PT) and Activated Partial Thromboplastin Time (aPTT) test parameters. The wound healing potentials were determined with the inhibition of hyaluronidase, collagenase and elastase enzymes. The TG showed antibacterial activity against Pseudomonas aeruginosa ATCC27853 and Escherichia coli ATCC25922. The results showed that TG and LBG possessed antioxidant properties including DPPH scavenging (21.0% and 17.6%, respectively) and H2O2 radical scavenging (59.4% and 79.0%, respectively) activities. The polysaccharides displayed significantly reducing PT and aPTT results. Between the two tested polysaccharides LBG showed significant hyaluronidase and collagenase inhibition activity at 10 mg/mL concentration. These findings show that these natural polysaccharides can be used to support of wound healing.Öğe Investigations of anti-aging potential of Hypericum origanifolium Willd. for skincare formulations(Elsevier, 2018) Boran, RukiyeSkin aging is caused by increased activation of extracellular matrix disruption enzymes, oxidative stress and DNA damage. Inhibition of these mechanisms by natural plants may be an encouraging approach to prevent skin aging. Hypericum is medically important plant and a source of several promising compounds. Nevertheless, there are no studies about the anti-aging potential of Hypericum origanifolium Willd (Guttiferae). The purpose of this study was to research the anti-collagenase, anti-elastase and anti-hyaluronidase effects, together with the antioxidant and genotoxic/antigenotoxic activities of H. origanifolium. Ethanol extract of H. origanifolium harvested from Turkey was tested for anti-collagenase, anti-elastase and anti-hyaluronidase activities. The extract inhibited collagenase and elastase activity. The highest ECM-degrade enzyme inhibition was demonstrated against collagenase (79.39%). The phenolic constituent and antioxidant activity were tested by Folin-Ciocalteu method (FCM), 2,2-dipenyl-1-picrylhydrazyl (DPPH) radical-scavenging and beta-carotene bleaching assay. The total phenol content revealed to be 93.4 +/- 1.6 mg GAE/g dry extract. IC50 values observed in DPPH and beta-carotene bleaching assays were 270 +/- 0.1 and 230 +/- 0.2 mu g/mL, respectively. Finally, the extract was investigated for its genotoxic/antigenotoxic effects using Ames Salmonella/microsome test system. Results indicated no sign of mutagenicity, and depending upon the concentration, the antigenotoxicity was noted with an inhibition of mutagenicity going from 21.54 to 84.90%. The results suggest that H. origanifolium can be considered as new natural sources to be potentially used as anti-aging ingredients in skin care formulations.Öğe Mentha longifolia (L.) ssp. longifolia essential oil: Source of natural antioxidant and antimutagen as food additive(Süleyman Demirel Üniversitesi, 2018) Boran, Rukiye; Uğur, AyselThis research was performed to control the antioxidant activity, mutagenicity and antimutagenic effect of Mentha longifolia (L.) ssp. longifolia essential oil (EO), which is considered as a possible ingredient when producing healthy food. The antiradical activity was established using DPPH (2,2-diphenyl-1- picrylhydrazyl radical) and ?-carotene/linoleic acid bleaching assays. The total phenolic content in the EO was evaluated by Folin Ciocalteau method (FCR). Ames Salmonella/microsome mutagenicity assay was applied to detect possible mutagenic and antimutagenic behavior. Our observations reveal that the IC50 value for DPPH radicals was 5.27 ± 0.13 mg/mL. The total antioxidant efficiency increased with an increase in the concentration of the EO, and IC50 value 11.7 ± 0.21 mg/mL. The total of phenolics was 186 ± 8.9 mg/g gallic acid equivalent/EO. Also, any concentrations of the EO used did not show mutagenic action but exhibited strong antimutagenic effects at 10.0-4.0 µg/plate concentrations. This research proposes that because of the antioxidant and antimutagenic characteristics, the EO is very advantageous and significant to the company’s manufacturing food additives.Öğe New lipase for biodiesel production: Partial purification and characterization of LipSB 25-4(Hindawi Publishing Corporation, 2014) Uğur, Aysel; Saraç, Nurdan; Boran, Rukiye; Ayaz, Berk; Ceylan, Özgür; Ökmen, GültenThe lipolytic activities of 300 Streptomyces isolates were determined in Tributyrin and Rhodamine-B Agar. Lipase activities were also measured with p-nitrophenyl palmitate (p-NPP) as a substrate. The strain of Streptomyces bambergiensis OC 25-4 used in this study was selected among 300 strains of Streptomyces from MUCC as the best lipase producer. The incubation conditions were optimized and the inoculum amount, incubation period, effect of carbon and nitrogen sources, and rates of MgSO4 and CaCO3 were investigated. LipSB 25-4 (the lipase produced by S. bambergiensis OC 25-4 strain) was partially purified with ammonium sulphate precipitation, dialysis, and gel filtration chromatography 2.73-fold and with 92.12 U/mg specific activity. The optimal pH and temperature for LipSB 25-4 were determined as 8.0 and 50°C, respectively. The lipase has high stability in all pH and temperature values used in this study. While LipSB 25-4 was slightly activated in the presence of ?-mercaptoethanol, it was slightly reduced by PMSF. The enzyme conserved approximately 75% of its activity at the end of 60 h, in the presence of methanol and ethanol. Since LipSB 25-4 displays high activity in the thermophilic conditions and stability in the presence of organic solvents, this lipase can catalyse the biodiesel production from olive oil by the transesterification reactions.Öğe Production and characterization of a cold-active and n-hexane activated lipase from a newly isolated Serratia grimesii RB06-22(Taylor & Francis, 2014) Uğur, Aysel; Boran, RukiyeA lipase-producing bacterium isolated from raw milk was identified as Serratia grimesii based on 16S rRNA sequence analysis. The extracellular lipase was partially purified by ammonium sulfate precipitation and ultrafiltration. Maximal activity was observed at 10 degrees C, the optimum pH was 8.0 and the enzyme was stable at 5-30 degrees C for 1 h. The K-m and V-max values were 1.7 mM and 0.3 mM/min respectively. It was found that the lipase had the highest hydrolytic activity towards sunflower oil and soybean oil. CaCl2 had a stimulatory effect on lipase activity, while EDTA and iodoacetic acid slightly inhibited the lipase activity and the enzyme was strongly inhibited by PMSF. The enzyme was compatible with various non-ionic surfactants as well as sodium cholate and saponin. In addition, the enzyme was relatively stable towards oxidizing agents. This lipase exhibited maximum activity in 35% n-hexane retaining about 2191% activity for 1 h.Öğe Purification and characterization of organic solvent-tolerant lipase from Streptomyces sp. OC119-7 for biodiesel production(Elsevier, 2015) Ayaz, Berk; Uğur, Aysel; Boran, RukiyeThis study determined the lipolytic activity of Streptomyces isolates and then purified and characterized the lipase obtained from Streptornyce.s sp. OC 119-7, the isolate demonstrated to have the high lipolytic activity. Ammonium sulfate precipitation and gel filtration chromatography were used to purify the extracellular alkaline lipase obtained from StTeptornyces sp. OC 119-7, and resulted in 5.52-fold purification with 68.055 U/mg specific activity. The enzyme showed optimal activity at pH 8.0 and 50 degrees C, with stability in a temperature range of 40-60 degrees C and at pHs of >= 7. Enzyme activity was enhanced by the presence of Ca2+ and Mg2+ and inhibited by the presence of Mn2+, Co2+, Cu2+, Zn2+, K+, Na+ and PMSF. OC 119-7 lipase displayed stability against surfactants and organic solvents. Lip0C 119-7 catalyzed transesterification of olive oil with methanol, suggesting that this lipase may be a potential enzymatic catalyst for biodiesel production. (C) 2014 Elsevier Ltd. All rights reserved.Öğe The mutagenic, antimutagenic and antioxidant properties of Hypericum lydium(TAYLOR & FRANCIS LTD, 2017) Boran, Rukiye; Uğur, AyselContext: There is a growing market demand for Hypericum sp., a pharmacologically active plant that has been traditionally used to treat various ailments. However, there have been limited studies on the extract or essential oil of Hypericum lydium Boiss (Hypericaceae). Objective: This study investigates for the first time the antioxidant, mutagenic and antimutagenic activity of an ethanol extract of H. lydium. Material and methods: Ethanol extract from aerial parts of H. lydium harvested from Turkey were tested for this mutagenic and antimutagenic activities (2.0-0.002 mg/plate) using Ames Salmonella/microsome test system. 4-Nitro-o-phenylenediamine (4-NPD) (3 mu g/plate) for the Salmonella typhimurium TA98 and sodium azide (NaN3) (8 mu g/plate) for the S. typhimurium TA100 were used as positive controls. The antioxidant activity, total antioxidant activity and phenolic constituent of the extract (2.0-0.002 mg/mL) was determined by the inhibition of 2,2-diphenyl-1-picrylhydrazyl radical (DPPH), beta-carotene-linoleic acid model and by means of Folin-Ciocalteu reagent, respectively. Results: The extract showed no sign of mutagenicity at the tested concentrations (0.002-2.0 mg/mL), and showed concentration-dependent antimutagenic activity against NaN3 and 4-NPD ranging from 26.8 to 81.5%. The extract was found to be an efficient scavenger of DPPH (IC50 0.165 +/- 0.23 mg/mL) and to inhibit beta-carotene-linoleic acid bleaching (IC50 0.39 +/- 0.11 mg/mL). Discussion and conclusion: These findings indicate ethanol extract of H. lydium to be a safe and effective agent that may be incorporated into new strategies for the prevention of cancer and mutagenesis.Öğe The Use of boron compounds for stabilization of lipase from pseudomonas aeruginosa ES3 for the detergent industry(SPRINGER HEIDELBERG, 2015) Saraç, Nurdan; Uğur, Aysel; Boran, Rukiye; Elgin, Emine SonayThis study aimed to characterize a lipase that is highly active and stable under typical washing conditions for use as a detergent ingredient by investigating the effects of various boron compounds on lipase stabilization under different conditions. In addition, the antimicrobial activity of the boron compounds used in enzyme stabilization was examined in order to obtain an effective antimicrobial detergent. A lipase-producing bacterium was isolated from kitchen wastewater samples using Rhodamine-B Agar medium and identified as Pseudomonas aeruginosa based on 16S rDNA sequence analysis. The ES3 lipase obtained from P. aeruginosa was purified, and the purified enzyme was found to have a molecular mass of 40 kDa. The enzyme showed optimal activity at pH 9.0-10.0 and 40 A degrees C and remained stable in the presence of various metal ions, surfactants and oxidizing agents. Moreover, the pH stability and thermostability of the enzyme was improved by the addition of boron compounds, which, when used as stabilizers in the incubation media, also increased the stability of the enzyme towards commercial detergents. Furthermore, the enzyme displayed properties comparable with the commercial product Lipolase(A (R)), which has shown excellent stability towards various commercial detergents. Finally, boron compounds used to stabilize the lipase were found to possess antimicrobial properties, suggesting that detergents incorporating these compounds will also exhibit antimicrobial activity when washing clothes and dishes.
