کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8360008 | 1542326 | 2015 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cloning, expression and structural stability of a cold-adapted β-galactosidase from Rahnella sp. R3
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کلمات کلیدی
β-galX-Gal5-bromo-4-chloro-3-indolyl-β-d-galactopyranosideONPONPGo-Nitrophenol - o-nitrofenolCold-adapted enzyme - آنزیم انعطاف پذیر سردortho-nitrophenyl-β-galactoside - اورات نیترو فنیل بتا گالاکتوزیدβ-galactosidase - بتا گالاکتوزیدازCircular dichroism spectroscopy - طیف سنجی دی کرومLactose hydrolysis - هیدرولیز لاکتوز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
A novel gene was isolated for the first time from a psychrophilic gram-negative bacterium Rahnella sp. R3. The gene encoded a cold-adapted β-galactosidase (R-β-Gal). Recombinant R-β-Gal was expressed in Escherichia coli BL21 (DE3), purified and characterized. R-β-gal belongs to the glycosyl hydrolase family 42. Circular dichroism spectrometry of the structural stability of R-β-Gal with respect to temperature indicated that the secondary structures of the enzyme were stable to 45 °C. In solution, the enzyme was a homo-trimer and was active at temperatures as low as 4 °C. The enzyme did not require the presence of metal ions to be active, but Mg2+, Mn2+, and Ca2+ enhanced its activity slightly, whereas Fe3+, Zn2+ and Al3+ appeared to inactive it. The purified enzyme displayed Km values of 6.5 mM for ONPG and 2.2 mM for lactose at 4 °C. These values were lower than the corresponding Kms reported for other cold-adapted β-Gals.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 115, November 2015, Pages 158-164
Journal: Protein Expression and Purification - Volume 115, November 2015, Pages 158-164
نویسندگان
Yuting Fan, Xiao Hua, Yuzhu Zhang, Yinghui Feng, Qiuyun Shen, Juan Dong, Wei Zhao, Wenbin Zhang, Zhengyu Jin, Ruijin Yang,