Sürdürülebilir Kalkınma Amaçları
Yayınlar
- MakaleAçık Erişim2020Bacteriocin producing bacteria isolated from Turkish traditional sausage samples
Erkaya, Elif; Genc, Berna; Akbulut, Sumeyya; Adiguzel, Gulsah; Omeroglu, Mehmet Akif; Ozkan, Hakan; Adiguzel, Ahmet
In this study, traditional sausage samples from different provinces of Turkey (Gaziantep, Antalya, erzurum and Kahramanmaras) were obtained and one hundred three isolates were collected. Using the (GTG)5-PCR genomic fingerprint analysis method, seven of them were observed to be different and conventional tests of these isolates were performed. Molecular identification of two isolates carrying the bacteriocin gene and having antimicrobial activity by agar disc diffusion method was performed by 16S rRNA sequence analysis. As a result, the seven isolates were identified as Aerococcus urinaeequi (EK1), Streptococcus salivarius (EK2), Leuconostoc mesenteroides (EK3), Macrococcus caseolyticus (EK4), Lactococcus garvieae (EK5), Staphylococcus saprophyticus (EK6) and Lactobacillus sakei (EK7). Among these strains, it has been determined that Ln. mesenteroides and L. sakei carried the mecentericin and sacacin genes. When antimicrobial activity against different strains was examined, inhibition formations of Ln. mesenteroides and L. sakei on Enterococcus faecalis, Shigella dysenteriae and Escherichia coli O157: H7 were observed.
- MakaleYalnız künye2019A novel endo-β-1,4-xylanase from Pediococcus acidilactici GC25; purification, characterization and application in clarification of fruit juices
Adiguzel, Gulsah; Faiz, Ozlem; Sisecioglu, Melda; Sari, Bilge; Baltaci, Ozkan; Akbulut, Sumeyya; Genc, Berna; Adiguzel, Ahmet
A 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 °C, respectively. The maximum activity was observed between 20 and 50 °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 Km and Vmax 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.