Characterization of a novel xylose isomerase from Anoxybacillus gonensis G2(T)

Yanmis D., Karaoglu H., Colak D. N., Sal F. A. Y., ÇANAKÇI S., BELDÜZ A. O.

TURKISH JOURNAL OF BIOLOGY, vol.38, no.5, pp.586-592, 2014 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 38 Issue: 5
  • Publication Date: 2014
  • Doi Number: 10.3906/biy-1403-76
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, TR DİZİN (ULAKBİM)
  • Page Numbers: pp.586-592
  • Recep Tayyip Erdoğan University Affiliated: Yes


The xylA gene encoding xylose isomerase from Anoxybacillus gonensis G2(T) has been cloned and successfully expressed in E. coli. Xylose isomerase was purified 10.98-fold by heat-shock and sequential column chromatography techniques to homogeneity, and the biochemical properties of the enzyme were characterized. The optimum temperature of the enzyme was 85 degrees C and maximum activity was observed at a pH of 6.5. Its Km and Vmax values were calculated as 25 +/- 2 mM and 0.12958 +/- 0.002 mu mol/min/mg protein, respectively. The effects of various metal ions on the xylose isomerase were examined. Divalent cations Co2+, Mg2+, and Mn2+ were essential for xylose isomerase activity; however, bivalent metal ions (Ca2+, Hg2+, Ni2+, Zn2+, Fe2+, and Cu2+) showed inhibitory effects. This is the first report of characterization of the xylose isomerase of Anoxybacillus spp. According to results obtained from this study, xylose isomerase is a promising candidate for industrial applications in production of xylulose and ribose.