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Journals / Turkish Journal of Biology / 2014 / Cilt: 38 - Sayı: 5

Characterization of a novel xylose isomerase from Anoxybacillus gonensis G2T

Derya YANMIŞ
Hakan KARAOĞLU
Dilşat Nigar ÇOLAK
Fulya AY ŞAL
Sabriye ÇANAKÇI
Ali Osman BELDÜZ
Pages
586–592
Publication Date
2014-05-01
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

According to results obtained from this study, xylose isomerase is a promising candidate for industrial applications in production of xylulose and ribose.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:The xylA gene encoding xylose isomerase from Anoxybacillus gonensis G2T has been cloned and successfully expressed in E. coli.
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Key Findings & Data: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.
💡
Conclusion & Impact:According to results obtained from this study, xylose isomerase is a promising candidate for industrial applications in production of xylulose and ribose.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Xylose isomerase · Anoxybacillus · characterization

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.

Özet

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.

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Cite This Article

YANMIŞ, D., KARAOĞLU, H., ÇOLAK, D. N., ŞAL, F. A., ÇANAKÇI, S., BELDÜZ, A. O. (2014). Characterization of a novel xylose isomerase from Anoxybacillus gonensis G2T. Turkish Journal of Biology, Cilt: 38 - Sayı: 5, 586–592. https://ajindex.com/articles/181677

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