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

Article Details

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

Publisher:

TUBITAK

Journal:

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

Document Type:

Article

Publication Date:

4/2014

Document Language:

Turkish

Document ID (Org No.):

2000812116

Frequency:

Bimonthly

eISSN:

1303-6092

pISSN:

1300-0152

Keywords:

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.

 

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.

Article Details

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

Publisher:

TUBITAK

Journal:

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

Document Type:

Article

Publication Date:

4/2014

Document Language:

Turkish

Document ID (Org No.):

2000812116

Frequency:

Bimonthly

eISSN:

1303-6092

pISSN:

1300-0152

Xylose isomerase

Anoxybacillus

characterization

thermophilic

Issues

Article Details

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

Publisher: TUBITAK

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

Document Type: Article

Publication Date: 4/2014

Document Language: Turkish

Document ID (Org No.): 2000812116

Frequency: Bimonthly

eISSN: 1303-6092

pISSN: 1300-0152

Xylose isomerase

Anoxybacillus

characterization

thermophilic

Issues

Authors:

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

Publisher:

TUBITAK

Journal:

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

Document Type:

Article

Publication Date:

4/2014

Document Language:

Turkish

Document ID (Org No.):

2000812116

Frequency:

Bimonthly

eISSN:

1303-6092

pISSN:

1300-0152