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2 →- MakaleAçık Erişim2019Scopus SJRQ3Biodiversity and characterization of gram-positive, catalase-positive cocci isolated from pastırma produced under different curing processes
Fettahoğlu, Kübra; Çinar, Kübra; Kaya, Mükerrem; Kaban, Güzin
The aim of this study was to determine the effects of different curing temperatures (4 °C or 10 °C) and agents (KNO3 or NaNO2) on microbiological and physicochemical properties of pastırma and diversity of gram-positive, catalase-positive cocci (GCC+) and also to investigate some technological properties of the strains. Four different groups of pastırma were produced applying different curing temperatures and agents. After production, GCC+ isolated from pastırma were subjected to phenotypic and genotypic (16S rRNA sequencing) identification. Genotypically characterized strains were evaluated for their technological properties. In all groups, aw and pH were observed to be under 0.90 and over 5.5, respectively. In genotypic identification, 45 isolates were identified as Staphylococcus vitulinus, while other isolates identified were S. equorum (n = 15), S. saprophyticus (n = 15), and S. xylosus (n = 12). All of the strains could grow at different salt concentrations (8% and 15%) and temperatures (4 °C, 10 °C, and 37 °C). Four strains of S. saprophyticus showed strong lipolytic activity while nine strains of S. vitulinus had strong proteolytic activity. This study showed that different curing temperatures and agents are particularly effective on the microflora in pastırma; however, these factors do not cause a high diversity in GCC+ in terms of species.
AtıfScopus6WoS6OpenAlex7TR Dizin2
İncele - MakaleAçık Erişim2012Scopus SJRQ3Changes in carbonic anhydrase activity and gene expression of Hsp70 in rainbow trout (Oncorhynchus mykiss) muscle after exposure to some metals
Söyüt, Hakan; Beydemir, Sükrü; Ceyhun, Saltuk Buǧrahan; Erdoǧan, Orhan; Kaya, Elif Duygu
The effects of some heavy metals Co(II), Cu(II), Zn(II), and Ag(I) on carbonic anhydrase (CA) activity from rainbow trout (RT) muscle were investigated. Moreover, the effects of these metals on the expression of heat shock protein 70 (Hsp70) gene in muscle tissue were examined by real-time quantitative PCR (RT-PCR) in muscle tissue aft er exposure to the metals at the end of 6, 12, 24, and 48 h. CA was purified with a specific activity of 2300 EU mg-1, a yield of 19%, and 1080-fold. The molecular weights (Mw) of subunit and native enzyme were approximately 30 and 31 kDa, respectively. Optimum pH, stable pH, optimum temperature, activation energy (Eα), activation enthalpy (ΔH), and Q10 (the difference in activity of enzyme caused by the increment of 10 oC) value were determined. Apparent Michaelis constant (Km), maximum reaction rate (Vmax), and turnover rate of the enzyme (Kcat) values were 1.29 mM, 0.17 μmol min-1, and 28.8 s-1, respectively. The catalytic efficiency (Kcat/Km) was 22.3. The heavy metals decreased in vitro CA activity. Inhibition mechanisms of the metal ions were noncompetitive, except for the Co(II) ion, which was competitive. The expression of the Hsp70 gene was increased in the presence of the metal ions. The expression level at the end of 48 h was the highest for all of the metals. Consequently, the in vitro inhibition rank order was determined as Co(II) > Zn(II) > Cu(II) > Ag(I). Interestingly, Ag(I) was the most effective metal ion on Hsp70 gene expression.
AtıfScopus9WoS8OpenAlex9İncele
Tam Kayıt
| Alan | Değer | Dil |
|---|---|---|
| creativeworkseries.issn | 1300-0128 | |
| dc.date.accessioned | 2026-10-29T19:11:26.257941732Z | |
| dc.date.available | 2026-10-29T19:11:26.257941732Z | |
| dc.identifier.uri | https://rdlopen.rawdatalibrary.net/r/bayburt/13773 | |
| dc.publisher | TUBITAK | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.title | Turkish Journal of Veterinary and Animal Sciences |

