Characterization of a xylanase from a thermophilic strain of Anoxybacillus pushchinoensis A8

Abstract: A facultatively anaerobic, thermophilic, xylanolytic bacterium was isolated from a sample collected from the Diyadin Hot Springs, Turkey. According to morphological, biochemical and molecular identification, this new strain was suggested to be representative of the Anoxybacillus pushchinoensis and it was designated as Anoxybacillus pushchinoensis strain A8. It exhibited 97% similarity to 16S rRNA gene sequence of A. pushchinoensis and 77% DNA homology by DNA-DNA hybridization studies. Q-sepharose and CM-sepharose chromatography was used to purify an extracellular xylanase to >90% purity from this species. The enzyme had a molecular mass of approximately 83 kDa. The enzyme showed optimum activity at pH 6.5 and it was 96% stable over a broad pH range of 6.5–11 for 24 hours. The enzyme had optimum activity at 55°C and it was 100% stable at temperature between 50–60°C up to 24 hours. Kinetic characterization of the enzyme was performed at temperature optima (55°C) and Vmax and K m were found to be 59.88 U/mg protein and 0.909 mg/mL, respectively. Oat spelt xylan but not xylooligosaccharides was degraded by the enzyme and xylose was the only product detected from oat xylan degradation. This suggested that the enzyme was an exo-acting xylanase.

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Characterization of a xylanase from a thermophilic strain of Anoxybacillus pushchinoensis A8 ; volume:63 ; number:5 ; year:2008 ; pages:599-606 ; extent:8
Biologia ; 63, Heft 5 (2008), 599-606 (gesamt 8)

Creator
Kacagan, Murat
Canakci, Sabriye
Sandalli, Cemal
Inan, Kadriye
Colak, Dilsat
Belduz, Ali

DOI
10.2478/s11756-008-0134-8
URN
urn:nbn:de:101:1-2409221606248.377556308457
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
15.08.0036, 6:25 AM CET

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Associated

  • Kacagan, Murat
  • Canakci, Sabriye
  • Sandalli, Cemal
  • Inan, Kadriye
  • Colak, Dilsat
  • Belduz, Ali

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