Production, purification, and characterization of a thermo-alkali stable and metal-tolerant carboxymethylcellulase from newly isolated Bacillus methylotrophicus Y37

YONCA DUMAN; YONCA YÜZÜGÜLLÜ KARAKUŞ; Arzu SERTEL; Fikriye POLAT

Makale detayları

Production, purification, and characterization of a thermo-alkali stable and metal-tolerant carboxymethylcellulase from newly isolated Bacillus methylotrophicus Y37

Yazarlar:

YONCA DUMAN | YONCA YÜZÜGÜLLÜ KARAKUŞ | Arzu SERTEL | Fikriye POLAT

Yayıncı:

TUBITAK

Ana Başlıklar:

Uygulamalı fizik

Dergi:

Turkish Journal of Chemistry 2016 Vol.40 Issue 5, pp.802-815

Belge Tipi:

Makale

Yayın Tarihi:

9/2016

Belge Dili:

İngilizce

Document ID (Org No.):

2000726556

Sıklık:

İki Aylık

eISSN:

1303-6130

pISSN:

1300-0527

Özet:

 

A carboxymethylcellulose (CMC)-degrading bacterium was isolated from soil, identified as Bacillus methylotrophicus according to the physiological properties and analyses of 16S rRNA and a partial sequence of the gyrase A (gyrA) gene, and named as B. methylotrophicus Y37. The CMCase enzyme was purified to homogeneity by 20.4-fold with 21.73% recovery using single-step hydrophobic interaction chromatography and biochemically characterized. CMCase showed a molecular weight of approximately 50 kDa as determined by SDS-PAGE. The activity profile of the CMCase enzyme exhibited optimum activity at 45 ∘∘^{\circ}C and pH 5.0. The activity was highly stable at alkaline pH levels. More than 90% of the original CMCase activity was maintained at relatively high temperatures ranging from 55 to 65 ∘∘^{\circ}C. The enzyme activity was induced by Ca2+2+^{2+}, Cd2+2+^{2+}, Co2+2+^{2+}, K++^{+}, Mg2+2+^{2+}, and Na1+1+^{1+}, whereas it was strongly inhibited by phenylmethanesulfonyl fluoride and iodoacetic acid. The enzyme tolerated Hg2+2+^{2+} up to 10 mM and presented hydrolytic activity towards glucan, filter paper, laminarin, and CMC but not ooo-nitrophenyl ββ\beta -D-galactopyranoside. Kinetic analysis of the purified enzyme showed Kmm_{m} and Vmaxmax_{max} values of 0.19 mg mL−1−1^{-1} and 7.46 U mL−1−1^{-1}, respectively. The biochemical properties of this CMCase make the enzyme a good candidate for many industrial applications.

Makale detayları

Production, purification, and characterization of a thermo-alkali stable and metal-tolerant carboxymethylcellulase from newly isolated Bacillus methylotrophicus Y37

Yazarlar: YONCA DUMAN | YONCA YÜZÜGÜLLÜ KARAKUŞ | Arzu SERTEL | Fikriye POLAT

Yayıncı: TUBITAK

Ana Başlıklar: Uygulamalı fizik

Dergi: Turkish Journal of Chemistry 2016 Vol.40 Issue 5, pp.802-815

Belge Tipi: Makale

Yayın Tarihi: 9/2016

Belge Dili: İngilizce

Document ID (Org No.): 2000726556

Sıklık: İki Aylık

eISSN: 1303-6130

pISSN: 1300-0527

Sayı

Yazarlar:

YONCA DUMAN | YONCA YÜZÜGÜLLÜ KARAKUŞ | Arzu SERTEL | Fikriye POLAT

Yayıncı:

TUBITAK

Ana Başlıklar:

Uygulamalı fizik

Dergi:

Turkish Journal of Chemistry 2016 Vol.40 Issue 5, pp.802-815

Belge Tipi:

Makale

Yayın Tarihi:

9/2016

Belge Dili:

İngilizce

Document ID (Org No.):

2000726556

Sıklık:

İki Aylık

eISSN:

1303-6130

pISSN:

1300-0527