- Turkish Journal of Biology
- Vol: 38 Issue: 5
- Characterization of a novel xylose isomerase from Anoxybacillus gonensis G2T
Characterization of a novel xylose isomerase from Anoxybacillus gonensis G2T
Authors : Derya Yanmiş, Hakan Karaoğlu, Dilşat Nigar Çolak, Fulya Ay Şal, Sabriye Çanakçi, Ali Osman Beldüz
Pages : 586-592
Doi:10.3906/biy-1403-76
View : 8 | Download : 2
Publication Date : 9999-12-31
Article Type : Makaleler
Abstract :The xylA gene encoding xylose isomerase from Anoxybacillus gonensis G2T 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 °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 mumol/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.Keywords : Xylose isomerase, Anoxybacillus, characterization, thermophilic