Yazarlar

• Akyol, I.(1)
• Kar, Bülent(1)
• Ozkose, E.(1)
• Torcan, Berat(1)
• Yazdic, F.C.(1)

• MakaleYalnız künye2025Scopus SJRQ3/r/munzur/1328
  Production and Partial Characterisation of Bifunctional Cellulase Genes of Anaerobic Gut Fungus Orpinomyces sp. GMLF19

  Yazdic, F.C.; Akyol, I.; Ozkose, E.

  Abstract: Fiber-degrading properties of anaerobic gut fungus, Orpinomyces sp. GMLF19, were investigated when it was grown on various carbon sources, namely carboxymethylcellulose, barley, oat, corncob and wheat straw. Fungi were developed under anaerobic conditions, and carboxymethylcellulase (CMCase), lichenase, and xylanase activities were determined by using DNS method. Meanwhile, the decreasing order of the enzyme activity of Orpinomyces sp. GMLF19 was observed to be lichenase > CMCase > xylanase. Relative activities of these enzymes in the isolate GMLF19 were found to be the highest when the culture was grown for 5 days. Cellulase gene domain was reproduced from chromosomal DNA and transferred into Escherichia coli with the aid of pCT plasmid vector and CMCase, lichenase and xylanase activities were determined using DNS method. The gene showed relatively higher CMCase activity and moderate lichenase activity while no xylanase activity was observed suggesting that the gene is bi-functional. The cell-associated activity of overexpressed Cel19 enzyme (E. coli cells containing this transferred gene were designated as C19) was relatively higher than extracellular activity. It was also recorded that this gene has 2 dockerin domains and 1 catalytic domain with the length of 1.585 bp, and it coded 50.59 kDa size of the protein which belongs to glycosyl hydrolase family 6.

  AtıfOpenAlex1

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• MakaleYalnız künye2023Scopus SJRQ2/r/munzur/2713
  Isolation, morphological identification, and xylanase characteristics of anaerobic gut fungi Neocallimastix from Anatolian wild goat

  Kar, Bülent; Torcan, Berat

  This study shows the morphological identification of anaerobic fungal strains isolated from fecal samples of goats inhabiting Turkey and the effects of various metal ions and chemicals on extracellular xylanase production. Three different anaerobic gut fungi isolated from wild goats in Turkey were identified as Neocallimastix spp. xylanase, cellulase, and lichenase production were tested in culture supernatants, and the maximum-specific activities were found as 560.42 ± 9.39, 159.70 ± 3.88, and 157.36 ± 3.83 (μmol/min/mg protein), respectively. While the optimum temperature range of exo-xylanases was found as 40–50°C, their optimum pH range was determined as 6.0–6.5. Xylanase activity decreased in metal ions and other chemical reactants based on dose. The metal ion that significantly inhibited xylanase activity was Fe+3. It was found that the ferric ions inhibited xylanase activity in all three anaerobic gut fungi by 30%–90% depending on molarity. On the contrary, the 1 mM concentrations of the Mn+2, Ba+2, Co+2, Cu+2, Sn+2, and Mg+2 metal ions and the ethylenediaminetetraacetic acid and β-mercaptoethanol reagents had a positive effect at rates in the range of 3%–92%. In conclusion, these findings demonstrate that anaerobic gut fungus has very stable fibrolytic enzymes that need to be separated, as well and the existence of a unique resource for industrial applications.

  AtıfScopus3·WoS3·OpenAlex4

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