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

Makale detayları

Characterization of a novel xylose isomerase from Anoxybacillus gonensis G2T

Yazarlar:

Derya YANMIŞ | Hakan KARAOĞLU | Dilşat Nigar ÇOLAK | Fulya AY ŞAL | Sabriye ÇANAKÇI | Ali Osman BELDÜZ

Yayıncı:

TUBITAK

Dergi:

Turkish Journal of Biology 2014 Vol.38 Issue 5, pp.586-592

Belge Tipi:

Makale

Yayın Tarihi:

4/2014

Belge Dili:

Türkçe

Document ID (Org No.):

2000812116

Sıklık:

İki Aylık

eISSN:

1303-6092

pISSN:

1300-0152

Anahtar kelimeler:

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.

 

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.

Makale detayları

Characterization of a novel xylose isomerase from Anoxybacillus gonensis G2T

Yazarlar:

Derya YANMIŞ | Hakan KARAOĞLU | Dilşat Nigar ÇOLAK | Fulya AY ŞAL | Sabriye ÇANAKÇI | Ali Osman BELDÜZ

Yayıncı:

TUBITAK

Dergi:

Turkish Journal of Biology 2014 Vol.38 Issue 5, pp.586-592

Belge Tipi:

Makale

Yayın Tarihi:

4/2014

Belge Dili:

Türkçe

Document ID (Org No.):

2000812116

Sıklık:

İki Aylık

eISSN:

1303-6092

pISSN:

1300-0152

Xylose isomerase

Anoxybacillus

characterization

thermophilic

Sayı

Makale detayları

Characterization of a novel xylose isomerase from Anoxybacillus gonensis G2T

Yazarlar: Derya YANMIŞ | Hakan KARAOĞLU | Dilşat Nigar ÇOLAK | Fulya AY ŞAL | Sabriye ÇANAKÇI | Ali Osman BELDÜZ

Yayıncı: TUBITAK

Dergi: Turkish Journal of Biology 2014 Vol.38 Issue 5, pp.586-592

Belge Tipi: Makale

Yayın Tarihi: 4/2014

Belge Dili: Türkçe

Document ID (Org No.): 2000812116

Sıklık: İki Aylık

eISSN: 1303-6092

pISSN: 1300-0152

Xylose isomerase

Anoxybacillus

characterization

thermophilic

Sayı

Yazarlar:

Derya YANMIŞ | Hakan KARAOĞLU | Dilşat Nigar ÇOLAK | Fulya AY ŞAL | Sabriye ÇANAKÇI | Ali Osman BELDÜZ

Yayıncı:

TUBITAK

Dergi:

Turkish Journal of Biology 2014 Vol.38 Issue 5, pp.586-592

Belge Tipi:

Makale

Yayın Tarihi:

4/2014

Belge Dili:

Türkçe

Document ID (Org No.):

2000812116

Sıklık:

İki Aylık

eISSN:

1303-6092

pISSN:

1300-0152