The effects of amoxicillin, cefazolin, and gentamicin antibiotics on the antioxidant system in mouse heart tissues

CIFTCI, MEHMET/0000-0002-1748-3729; KOCPINAR, ENVER FEHIM/0000-0002-6031-4664; Budak, Harun/0000-0002-7371-8959; Sisecioglu, Melda/0000-0002-1127-0570WOS:000560347900005PubMed: 31721686Background: Free radicals lead to destruction in various organs of the organism. The improper use of antibiotics increases the formation of free radicals and causes oxidative stress. Objective: In this study, it was aimed to determine the effects of gentamicin, amoxicillin, and cefazolin antibiotics on the mouse heart. Methods: 20 male mice were divided into 4 groups (1st control, 2nd amoxicillin, 3rd cefazolin, and 4th gentamicin groups). The mice in the experimental groups were administered antibiotics intraperitoneally at a dose of 100 mg / kg for 6 days. The control group received normal saline in the same way. The gene expression levels and enzyme activities of SOD, CAT, GPx, GR, GST, and G6PD antioxidant enzymes were investigated. Results: GSH levels decreased in both the amoxicillin and cefazolin groups, while GR, CAT, and SOD enzyme activities increased. In the amoxicillin group, Gr, Gst, Cat, and Sod gene expression levels increased. Conclusion: As a result, it was concluded that amoxicillin and cefazolin caused oxidative stress in the heart, however, gentamicin did not cause any effects.Scientific Research Project of Ataturk University of TurkeyAtaturk University [PRJ2013/296]This work was supported by a grant from the Scientific Research Project of Ataturk University of Turkey [Grant Number: PRJ2013/296]

Purification and biochemical characterization of a novel thermostable serine alkaline protease from Aeribacillus pallidus C10: a potential additive for detergents

An extracellular thermostable alkaline serine protease enzyme from Aeribacillus pallidus C10 (GenBank No: KC333049), was purified 4.85 and 17. 32-fold with a yield of 26.9 and 19.56%, respectively, through DE52 anion exchange and Probond affinity chromatography. The molecular mass of the enzyme was determined through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with approximately 38.35 kDa. The enzyme exhibited optimum activity at pH 9 and at temperature 60 °C. It was determined that the enzyme had remained stable at the range of pH 7.0–10.0, and that it had preserved more than 80% of its activity at a broad temperature range (20–80 °C). The enzyme activity was found to retain more than 70% and 55% in the presence of organic solvents and commercial detergents, respectively. In addition, it was observed that the enzyme activity had increased in the presence of 5% SDS. KM and Vmax values were calculated as 0.197 mg/mL and 7.29 μmol.mL−1.min−1, respectively

New xylanolytic enzyme from Geobacillus galactosidasius BS61 from a geothermal resource in Turkey

Adiguzel, Ahmet/0000-0001-8848-6647; GENC, BERNA/0000-0002-2790-9578WOS: 000447682100113PubMed: 30059740In this study, isolation, conventional and molecular characterizations of ten thermophilic bacteria from Rize/Ayder were carried out. Xylanase from Geobacillus galactosidasius BS61 (GenBank number: 10(447660) 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 degrees 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. K-m and V-max 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 HPO42- 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. (C) 2018 Elsevier B.V. All rights reserved.Research Development Centre of Ataturk UniversityAtaturk University [2015-339, FAD-2018-6352]This work was supported by the Research Development Centre of Ataturk University (Grant numbers are 2015-339 and FAD-2018-6352)

A novel endo-beta-1,4-xylanase from Pediococcus acidilactici GC25; purification, characterization and application in clarification of fruit juices

GENC, BERNA/0000-0002-2790-9578; Adiguzel, Ahmet/0000-0001-8848-6647WOS: 000466621200059PubMed: 30753879A 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 degrees C, respectively. the maximum activity was observed between 20 and 50 degrees 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 K-m and V-max 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. (C) 2019 Elsevier B.V. All rights reserved.Research Development Center of Ataturk UniversityAtaturk University [2015/54, FAD-2018-6352]; Ataturk University, TurkeyAtaturk UniversityThis research was conducted under the projects numbered 2015/54 and FAD-2018-6352 supported by the Research Development Center of Ataturk University. the authors acknowledged the support of Ataturk University, Turkey for this work