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Dergiler / 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
Sayfa
586–592
Yayın Tarihi
2014-05-01
DOI
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⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

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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Amaç & Hipotez:The xylA gene encoding xylose isomerase from Anoxybacillus gonensis G2T has been cloned and successfully expressed in E. coli.
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Temel Bulgular & Veri: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.
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Sonuç & Katkı:According to results obtained from this study, xylose isomerase is a promising candidate for industrial applications in production of xylulose and ribose.
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Xylose isomerase · Anoxybacillus · characterization

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.

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.

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Bu Makaleye Atıf Yap

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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Kaynakça (15)

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