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Your search keyword '"Ekrem Köksal"' showing total 4 results
Start Over Author "Ekrem Köksal" Journal international journal of food properties
4 results on '"Ekrem Köksal"'

1. Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)

Author

Ahmet Altay, Tubanur Koktepe, Lokman Durmaz, Fevzi Topal, İlhami Gülçin, and Ekrem Köksal

Subjects
Cress (Lepidium sativum), peroxidase, enzyme purification, enzyme characterization, enzyme inhabitation, Nutrition. Foods and food supply, TX341-641, Food processing and manufacture, TP368-456
Abstract

Cress (Lepidium sativum) is an annual herb from Brassicaceae family, and in some regions. It is known as peppergrass, garden cress, garden peppercress, pepperwort, or poor man’s pepper. Cress is an important medicinal plant in some countries including Turkey. This plant has major scientific and therapeutic significance. Peroxidase (POD, E.C.1.11.1.7) is an oxidoreductase enzyme produced by a number of organisms. In this study, POD enzyme was purified from cress by ammonium sulphate precipitation, gel filtration, and CM-Sephadex ion-exchange chromatographies. Km and Vmax values were calculated from the Lineweaver-Burk graph for H2O2 and guaiacol substrates and the substrate specificity of POD was investigated. The results showed that substrate specificity of H2O2 is better than substrate specificity of guaiacol for this enzyme. The inhibition effects of three cations (Al3+, Cu2+, and Cr3+) and one organic compound of cetyl trimethylammonium bromide were performed and their inhibition types were determined. Finally, optimum pH, optimum temperature, optimum ionic strength, and stable pH were determined.

Published
2018
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2. Purification, characterization and selected inhibition properties of peroxidase from haricot bean (Phaseolus vulgaris L.)

Author

Ekrem Köksal, Sevgi Altın, İlhami Gülçin, Hatice Tohma, Tubanur Koktepe, and EBYÜ, Fen Edebiyat Fakültesi

Subjects
inorganic chemicals, 01 natural sciences, 0404 agricultural biotechnology, Haricot bean (Phaseolus vulgaris), Enzyme purification, Peroxidase, chemistry.chemical_classification, biology, 010405 organic chemistry, Precipitation (chemistry), Cationic polymerization, food and beverages, 04 agricultural and veterinary sciences, Enzyme characterization, biology.organism_classification, 040401 food science, 0104 chemical sciences, Enzyme inhibition, Point of delivery, Enzyme, chemistry, Biochemistry, biology.protein, Phaseolus, Food Science
Abstract

In this study, a cationic soluble peroxidase (POD) was homogeneously purified and biochemically characterized. The enzyme purification involved the combination of (NH4)2SO4 precipitation, CM-Sephadex cation exchange, and gel filtration chromatography. The purity of the enzyme was examined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, and one single prominent band was obtained with a molecular weight of approximately 45 kDa. The thermal and pH stability showed that the enzyme was stable at pH 5.0 and at 40°C, respectively. The activity remained stable at pH 4.0 at least for 10 days. Km and Vmax values were calculated from Lineweaver–Burk graph for each substrate. POD exhibited Km values of 0.0154 and 0.065 mM for guaiacol and H2O2, respectively. The enzyme was highly inhibited by sodium azide. This study could enrich the literature regarding the properties of POD from haricot bean that could be applicable to biomedical analysis.

Published
2017
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3. Purification, characterization, and inhibition sensitivity of peroxidase from wheat (Triticum aestivum ssp. vulgare)

Author

Ekrem Köksal, İlhami Gülçin, Hatice Tohma, and Sevgi Altın

Subjects
0301 basic medicine, Chromatography, biology, Molecular mass, 010405 organic chemistry, Size-exclusion chromatography, Substrate (chemistry), 01 natural sciences, 0104 chemical sciences, 03 medical and health sciences, chemistry.chemical_compound, 030104 developmental biology, chemistry, biology.protein, Enzyme kinetics, Guaiacol, Hydrogen peroxide, Polyacrylamide gel electrophoresis, Food Science, Peroxidase
Abstract

The purification and characterization of peroxidase is currently growing interests since peroxidases have implications in various industrial and biochemical applications. In this study, wheat peroxidase was purified using (NH4)2SO4 precipitation, CM-Sephadex cation exchange, and gel filtration chromatographies. Enzyme purity and molecular mass were checked by sodium dodecyl sulphate polyacrylamide gel electrophoresis. Enzyme kinetics was studied using two substrates: guaiacol and hydrogen peroxide (H2O2). Km and Vmax values were calculated from Lineweaver-Burk graph for each substrate. Wheat peroxidase activity has been enhanced 284-fold. Wheat peroxidase had molecular mass of 38.8 kDa. Km values for guaiacol and H2O2 were found as 2.467 mM and 7.307 mM, respectively. The pH and temperature optima were 5.5 and 40.0°C, respectively. Also, the enzyme was highly inhibited by citric acid and Cetyltrimethylammonium bromide.

Published
2017
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4. Anticholinergic and antioxidant activities of avocado (Folium perseae) leaves – phytochemical content by LC-MS/MS analysis

Author

Leyla Polat Kose, Zeynebe Bingol, Ruya Kaya, Ahmet C. Goren, Hulya Akincioglu, Lokman Durmaz, Ekrem Koksal, Saleh H. Alwasel, and İlhami Gülçin

Subjects
avocado, folium perseae, antioxidant activity, radical scavenging, acetylcholinesterase, butyrylcholinesterase, Nutrition. Foods and food supply, TX341-641, Food processing and manufacture, TP368-456
Abstract

In the first stage of the manuscript, we aimed to examine antioxidant capacity and anticholinergic properties of avocado (Folium perseae) leaves. Avocado leaf was extracted by water (WEFP) and ethyl alcohol (EEFP) and antioxidant activity was determined using by several antioxidant assays including DPPH· and ABTS•+ radical scavenging assays, Cu2+-Cu+ reducing, Fe3+-Fe2+ reducing, and FRAP reducing activities. Avocado leaf extracts demonstrated antioxidant activity and anticholinergic activities, while α-tocopherol, BHT, trolox, and BHA were used as positive antioxidant controls. In the second part of this study, the inhibition effects of WEFP and EEFP were valuated against acetylcholinesterase and butyrylcholinesterase enzymes, which catalyze the breakdown of choline esters (i.e. neurotransmitters). This study obviously showed that avocado leaf extracts had effective antioxidant, antiradical, and anticholinergic influences.

Published
2020
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