POLYSACCHARIDASE AND GLYCOSIDASE PRODUCTION OF AVICEL GROWN RUMEN FUNGUS ORPINOMYCES SP GMLF5

Comlekcioglu U., Ozkose E., Yazdic F. C., Akyol İ., Ekinci M. S.

ACTA BIOLOGICA HUNGARICA, cilt.61, sa.3, ss.333-343, 2010 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 61 Sayı: 3
  • Basım Tarihi: 2010
  • Doi Numarası: 10.1556/abiol.61.2010.3.9
  • Dergi Adı: ACTA BIOLOGICA HUNGARICA
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.333-343
  • Anahtar Kelimeler: Orpinomyces, avicel, degradation, polysaccharidase, glycosidase, NEOCALLIMASTIX-FRONTALIS, ANAEROBIC FUNGI, CAECOMYCES-COMMUNIS, ESCHERICHIA-COLI, STRAIN PC-2, XYLANASE, ENZYMES, DEGRADATION, CELLULASES, CELLULOSE
  • Ankara Üniversitesi Adresli: Hayır

Özet

Extracellular and cell-associated enzyme preparations were obtained from ruminal anaerobic fungi Orpinomyces sp. GMLF5 grown in culture containing microcrystalline cellulose (avicel) as sole energy source and degradation capacities of the preparations towards several polysaccharides and glycosides were studied. Fungus showed substantial increases in xylanase, carboxymethyl cellulase (CMCase), lichenase, amylase, beta-xylosidase, beta-glucosidase and alpha-L-arabinofuranosidase activities between 72 and 168 hours. High amounts of cell associated beta-xylosidase were noted in 4 and 5 days old cultures. Optimum temperature and pH of the polysaccharidases were found at 50 degrees C and 6.0-6.5, respectively. Xylanase was found to be virtually stable at 50 degrees C, CMCase and lichenase were stable at 40 degrees C for 200 min, however amylase was found more sensitive to heat treatment. The fibrolytic enzymes of the isolate GMLF5 were observed to be capable of hydrolyze the avicel.