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Author

Ebru Oztas Gulmus

Bio: Ebru Oztas Gulmus is an academic researcher from Erzurum Technical University. The author has contributed to research in topics: Protease & Thauera. The author has an hindex of 2, co-authored 2 publications receiving 15 citations.
Topics: Protease, Thauera, Thermophile, Enzyme assay, Bacteria

Papers
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Journal ArticleDOI
TL;DR: The results of the study indicated that these bacteria and their enzymes can be used as a source of industrial enzymes.
Abstract: The aim of present study was the isolation and characterization of thermophilic bacteria from three different hot springs in Erzurum, Turkey. For this purpose, 85 bacteria were isolated and characterized by ERIC-PCR genomic fingerprinting and classical identification methods such as morphological, physiological and biochemical characteristics. According to the results, 29 bacterial isolates with different band profiles were analyzed by 16S rRNA gene sequencing and identified as belonging to the genus of Bacillus, Pseudomonas, Silanimonas, Thermomonas and Thauera. This is the first report on the isolation of Silanimonas lenta, Thauera sp. and Thermomonas haemolytica from Turkey Hot Springs. The amylase, lipase and protease enzyme production potentials of the isolates were 80%, 91.25% and 81.25%, respectively. Moreover, 56.47% of the isolates (48) were able to produce all of these enzymes. Therefore, the results of the study indicated that these bacteria and their enzymes can be used as a source of industrial enzymes.

15 citations

Journal ArticleDOI
TL;DR: According to results obtained from this study, this new strain of Thermomonas haemolytica isolated from geothermal Nenehatun hot spring in Turkey is a promising candidate for industrial applications in production of detergent.
Abstract: In this study, it was aimed to determine the ability to produce protease enzyme of Thermomonas haemolytica isolated from geothermal Nenehatun hot spring in Turkey and utilization of this enzyme in the detergent industry to remove protein stains. The protease-producing strains were screened from hot springs, and a potential strain was identified as T. haemolytica according to morphological, physiological and biochemical characteristics and sequence of 16S rRNA gene. Maximum protease activity was observed at 55 °C and pH 9.0 at 72 h of incubation. Activity was very stable between 50 and 65 °C and pH 8.0–10.0, respectively. The enzyme activity was significantly inhibited by PMSF and partly inhibited by EDTA, EGTA, SDS, and urea. Some divalent metal ions such as Ca2+, Mg2+, and Mn2+ increased the enzyme activity, while Zn2+ and Cu2+ decreased. Michaelis–Menten constant (Km) and maximum velocity (Vmax) values were calculated by Lineweaver–Burk plot as 125 EU/ml and 1262 mg/ml, respectively. The biochemical characterization of the protease obtained from T. haemolytica was performed and applied on the blood and grass-stained fabrics with detergent to evaluate the stain removal performance of the enzyme. It was observed that the application of detergent with enzyme was more effective than the detergent without enzyme to clean up the stained fabrics. This is the first report of characterization of the protease of T. haemolytica. According to results obtained from this study, this new strain is a promising candidate for industrial applications in production of detergent.

14 citations


Cited by
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Journal ArticleDOI
Emmanuel Quayson1, Jerome Amoah, Shinji Hama, Akihiko Kondo1, Chiaki Ogino1 
TL;DR: This review presents a way forward to address immobilized lipase cost by using green chemistry strategies that have shown success in recent studies to supplant chemical catalysts currently used in biodiesel production.
Abstract: As green catalysts, lipases' productivity, and wide substrate selectivity are preferable over chemical catalysts in biodiesel production. Lipases require milder reaction conditions and produce cleaner downstream products. To ensure practical recovery of lipases for repeated uses in biodiesel production, immobilizing lipases into solid forms has been suggested to complement its efficiency, utility, and sustainability. Immobilization, however, adds to the cost of the already economically inviable lipases. Most immobilization protocols also largely depend on fossil derivatives and produce an ever-increasing amount of waste. Therefore, it has been deemed necessary to delineate a scope for the fundamental success of using immobilized lipases for large-scale biodiesel production. Hence, this review presents a way forward to address immobilized lipase cost by using green chemistry strategies that have shown success in recent studies. A comparison of lipases with other biodiesel catalysts is presented in the early part of this review. Conventional and emerging immobilization protocols are also evaluated. The choice between synthetic and natural polymers for immobilization emphasizes the importance of using green chemistry metrics in addressing reusability, toxicity, resource efficiency, water, and carbon footprint of lipase immobilization. Therefore, this review advances immobilized lipase technology by identifying gaps that can be used by research and industry for its deployment to supplant chemical catalysts currently used in biodiesel production.

58 citations

Journal ArticleDOI
TL;DR: In this article, a high compatible thermoalkaliphilic lipase (TA) with detergents from new thermophilic bacterial strains utilizing fish wastes for industrial application was produced.

27 citations

Journal ArticleDOI
TL;DR: In this paper, the enzyme performance was further optimized to reach 22.903U/mL with an overall optimization fold of 46.7, achieved under the optimized fermentation medium composed of (%) molasses; 8, (NH4)2SO4; 0.45, wheat bran; 5, MgSO4·7H2O; 0., NaCl; 0, NaCl, 0.15, 231.05 and 57.206min−1 respectively.
Abstract: The growing industrial applications of alkaline proteases urged the production of highly active stable enzymes. In the current study, the enzyme production was achieved by submerged fermentation using the bacterial strain Bacillus licheniformis ALW1 that was further optimized to reach 22.903U/mL. The overall optimization fold was 46.7, achieved under the optimized fermentation medium composed of (%) molasses; 8, (NH4)2SO4; 0.45, wheat bran; 5, MgSO4·7H2O; 0.2, KH2PO4; 0.4, NaCl; 0.2 adjusted at pH 8 and incubated for 7days at 37 °C and 280 rpm. Additionally, the enzyme activity after partial purification was optimized by studying the effect of pH and temperature as well as the substrate concentration. The results indicated that the enzyme optimum activity was achieved at pH 9 and 70 °C with Km, Vmax and Kcat values of 3.846 mg/mL, 76.923U/mL/min and 1.206min−1 respectively. Thermal stability study of the partial pure enzyme indicated the half live times of the enzyme as 693.15, 231.05 and 57.76 min−1 at 55, 60 and 65 °C respectively, confirming its thermo-stability. Finally, the efficacy of the partial pure enzyme as a detergent additive was examined. The enzyme retained more than 80% of its activity with an efficient washing performance in the removal of blood stain after 30 min at 50 °C in addition to a commercial detergent.

24 citations

Journal ArticleDOI
TL;DR: In this paper, traditional chemical methods used for shrink resist finishing are suffering from some drawback, which has negative impacts on the performance attributes of the yarn and its performance is not improved by these methods.
Abstract: Felting shrinkage of wool is a major problem which has negative impacts on its performance attributes. Traditional chemical methods used for shrink-resist finishing are suffering from some drawback...

16 citations

Journal ArticleDOI
TL;DR: The results of the study indicated that these bacteria and their enzymes can be used as a source of industrial enzymes.
Abstract: The aim of present study was the isolation and characterization of thermophilic bacteria from three different hot springs in Erzurum, Turkey. For this purpose, 85 bacteria were isolated and characterized by ERIC-PCR genomic fingerprinting and classical identification methods such as morphological, physiological and biochemical characteristics. According to the results, 29 bacterial isolates with different band profiles were analyzed by 16S rRNA gene sequencing and identified as belonging to the genus of Bacillus, Pseudomonas, Silanimonas, Thermomonas and Thauera. This is the first report on the isolation of Silanimonas lenta, Thauera sp. and Thermomonas haemolytica from Turkey Hot Springs. The amylase, lipase and protease enzyme production potentials of the isolates were 80%, 91.25% and 81.25%, respectively. Moreover, 56.47% of the isolates (48) were able to produce all of these enzymes. Therefore, the results of the study indicated that these bacteria and their enzymes can be used as a source of industrial enzymes.

15 citations