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

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Publication Date : 2014-12-01

Article Type : Research Paper

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 insert ignore into journalissuearticles values(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